Cytokines

Pigment epithelium-derived factor (PEDF) is encoded by the SERPINF1 gene in humans and found in verebrates. It is a secreted phosphoglycoprotein that belongs to the clade F subfamily, serpin superfamily of proteinase inhibitors. The PEDF is a noninhibitory serpin with neurotrophic, anti-angiogenic, and anti-tumorigenic properties. It is synthesized as a 418 a.a. about 50kDa precursor that contains a 19 a.a. signal sequence and a 399 a.a. mature region that shows a pyroglutamate at Gln20. Like other serpins, it contains three β-sheets, 810 α-helices, and a C-terminal RCL (reactive center loop). Unlike other serpins with Ser protease inhibiting activity. PEDF has functions of inducing extensive neuronal differentiation in retinoblastoma cells, inhibiting of angiogenesis. As it does not undergo the S (stressed) to R (relaxed) conformational transition characteristic of active serpins, it exhibits no serine protease inhibitory activity. PEDF is researched as a therapeutic candidate for treatment of such conditions as choroidal neovascularization, heart disease, and cancer.   Product Properties   Synonyms Serpin peptidase inhibitor, clade F，member 1,SerpinF1, EPC-1, Cell proliferation-inducing gene 35  protein Accession P36955 GeneID 5176 Source E.coli-derived human Pigment Epithelium-derived Factor protein,Gln20-Pro418 Molecular Weight Approximately 44.4 KDa AA Sequence QNPASPPEEG SPDPDSTGAL VEEEDPFFKV PVNKLAAAVS NFGYDLYRVR SSTSPTTNVL LSPLSVATAL SALSLGAEQR TESIIHRALY YDLISSPDIH GTYKELLDTV TAPQKNLKSA SRIVFEKKLR IKSSFVAPLE KSYGTRPRVL TGNPRLDLQE INNWVQAQMK GKLARSTKEI PDEISILLLG VAHFKGQWVT KFDSRKTSLE DFYLDEERTV RVPMMSDPKA VLRYGLDSDL SCKIAQLPLT GSMSIIFFLP LKVTQNLTLI EESLTSEFIH DIDRELKTVQ AVLTVPKLKL SYEGEVTKSL QEMKLQSLFD SPDFSKITGK PIKLTQVEHR AGFEWNEDGA GTTPSPGLQP AHLTFPLDYH LNQPFIFVLR DTDTGALLFI GKILDPRGP Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97 % by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The ED50 as determined by its ability to enhance the adhesion of human Saos2 cells to bovine Collagen I coated plate is less than 2 ng/ml, corresponding to a specific activity of > 5.0 × 10 5 IU/mg. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM PB, pH 7.4, 150 mM NaCl. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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PlGF-2 is an angiogenic factor that belongs to the cysteine-knot superfamily of growth factors. PlGF-2 is expressed in umbilical vein endothelial cells and placenta. It signals through the VEGFR-1/FLT1 receptor, and stimulates endothelial cell proliferation and migration. PlGF-2 also signals through Neuropilin (NP-1), and can bind with high affinity to heparin. Recombinant Human PlGF-2 is a 34.6 kDa disulfide-linked homodimeric protein of two 152 amino acid polypeptide chains.   Product Properties   Synonyms Placenta Growth Factor-2, PGFL Accession P49763-3 GeneID 5228 Source E.coli-derived Human PlGF-2 protein,Leu19-Arg131. Molecular Weight Approximately 34.6 kDa. AA Sequence LPAVPPQQWA LSAGNGSSEV EVVPFQEVWG RSYCRALERL VDVVSEYPSE VEHMFSPSCV SLLRCTGCCG DENLHCVPVE TANVTMQLLK IRSGDRPSYV ELTFSQHVRC ECRPLREKMK PERRRPKGRG KRRREKQRPT DCHLCGDAVP RR Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97% by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The biologically active as determined by its ability to chemoattract human monocytes using a concentration range of 5.0-50 ng/mL. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4, with 0.02 % Tween-20. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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CXCL4, also called PF4 (platelet factor 4), is an 8 kDa member of the CXC chemokine family, sharing features with CXCL8/IL-8 and CXCL7/NAP-2. Mature human CXCL4 shares 65-76% amino acid sequence identity with mouse, rat, bovine, ovine and porcine CXCL4. The active protein is a tetramer of CXCL4 subunits that forms a ring of heparin-binding positive charges from sites at the C-terminal region of each monomer. Megakaryocytes synthesize CXCL4 and store it in platelet alpha -granules. Secretion from activated platelets can produce micromolar levels in serum and over 100-fold higher within clots. In contrast to other CXC chemokines, CXCL4 does not contain an ELR motif and lacks binding to nearly all chemokine receptors. A potential high-affinity G-protein-coupled receptor for CXCL4, the CXCR3 isoform CXCR3B, is expressed in human but not mouse. In most cases, it is likely that cell surface binding and signaling properties of CXCL4 are due to binding of glycosaminoglycans chains, particularly chondroitin sulfates. CXCL4 released from activated platelets binds and regulates thrombin/thrombomodulin complexes, regulates and enhances production of activated Protein C (APC), and limits the coagulation cascade. It binds and influences the enzymatic activity of coagulation factor Xa. It binds fibrin and affects clot structure. Therapeutic doses of the anticoagulant heparin neutralize CXCL4 procoagulant effects.   Product Properties   Synonyms Iroplact, Oncostatin-A Accession P02776 GeneID 5196 Source E.coli-derived Human GRO-γ,Glu32-Ser101. Molecular Weight Approximately 7.8 kDa AA Sequence EAEEDGDLQC LCVKTTSQVR PRHITSLEVI KAGPHCPTAQ LIATLKNGRK ICLDLQAPLY KKIIKKLLES Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97% by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The biological activity determined by a chemotaxis bioassay using human fibroblasts is in a concentration of 1.0-10 ng/mL. Endotoxin < 1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in Acetonitrile and TFA Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycle. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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PDGF is involved in a number of biological processes, including hyperplasia, embryonic neuron development, chemotaxis, and respiratory tubule epithelial cell development. The A-chain homodimers of the platelet-derived growth factor (PDGF AA) are widely expressed in normal and transformed cells. The mitogenic properties of PDGF AA are well established. FGF-2 and platelet-derived growth factor-A (PDGF-AA) are potent modulators of oligodendrocytes, the main responsible cells for myelin   Product Properties   Synonyms PDGF1, PDGF-A, PDGFAA, PDGF-AA Accession P04085 GeneID 5154 Source E.coli-derived human PDGF-AA, Ser87-His211, with an N-terminal Met. Molecular Weight Approximately 28.8 kDa. AA Sequence MSIEEAVPAV CKTRTVIYEI PRSQVDPTSA NFLIWPPCVE VKRCTGCCNT SSVKCQPSRV HHRSVKVAKV EYVRKKPKLK EVQVRLEEHL ECACATTSLN PDYREEDTGR PRESGKKRKR KRLKPT Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >95% by SDS-PAGE analyses. Biological Activity The ED50 for this effect is 50-200 ng/mL in a fluorometric assay using the redox sensitive dye. Measured in a cell proliferation assay using NR6R-3T3 mouse fibroblast cells. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM PB, 300 mM NaCl, pH 6.0. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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Platelet-derived growth factor (PDGF) was discovered as a major mitogenic factor present in serum but absent from plasma. In vitro, PDGF-BB stimulated MAP kinase activity and cell motility of isolated lymphatic endothelial cells. In vivo, PDGF-BB potently induced growth of lymphatic vessels. Expression of PDGF-BB in murine fibrosarcoma cells induced tumor lymphangiogenesis, leading to enhanced metastasis in lymph nodes. The PDGF signaling system contributes to and vascular remodeling. Growth factors such as PDGF exert potent effects on wound healing including the regeneration of tooth-supporting structures.   Product Properties   Synonyms Becaplermin, ODGF, PDGF-2, PDGFBB, PDGF-BB Accession P01127 GeneID 5155 Source E.coli-derived human PDGF-BB protein, Ser82-Thr190, with an N-terminal Met. Molecular Weight Approximately 24.8 kDa AA Sequence MSLGSLTIAE PAMIAECKTR TEVFEISRRL IDRTNANFLV WPPCVEVQRC SGCCNNRNVQ CRPTQVQLRP VQVRKIEIVR KKPIFKKATV TLEDHLACKC ETVAAARPVT Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97 % by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 3 ng/ml, corresponding to a specific activity of > 3.3 × 10^5 IU/mg. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. For your safety and health, please wear lab coats and disposable gloves for operation. 2. For research use only.

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Syndecan-4, previously known as amphiglycan or ryudocan, is a member of the syndecan family of Type 1 transmembrane proteins capable of carrying heparan sulfate (HS) and chondroitin sulfate glycosaminoglycans. Human Syndecan-4 ECD shares  approximately 79%, 78% and 81% aa identity with mouse, rat and porcine Syndecan-4 ECD, respectively. Syndecans are the best-characterized plasma membrane proteoglycans with two conserved cytoplasmic domains and divergent extracellular portions, except for HS attachment sites. SYND4 is the most similar to SYND2, but is more universally expressed and is found in virtually every cell type. Expression can be upregulated by TGFβ2 and in response to mechanical stress in smooth muscle, wound healing, arterial injury or acute myocardial infarction, probably in response to at least one inflammatory mediator. SYND4 has more widespread distribution than other syndecans and it is the only syndecan that has been found consistently in focal adhesions.   Product Properties Synonyms Amphiglycan, MGC22217, Ryudocan, SDC4, syndecan 4, Syndecan4 Accession P31431 GeneID 6385 Source E.coli-derived human SYND4 protein, Glu19-Glu145 Molecular Weight Approximately 13.9 kDa. AA Sequence ESIRETEVID PQDLLEGRYF SGALPDDEDV VGPGQESDDF ELSGSGDLDD LEDSMIGPEV VHPLVPLDNH IPERAGSGSQ VPTEPKKLEE NEVIPKRISP VEESEDVSNK VSMSSTVQGS NIFERTE Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95 % by SDS-PAGE and HPLC analyses. Biological Activity The specific activity is determined by binding ability in a functional ELISA. Immobilized recombinant human SYND4 at 500 ng/mL (100 μl/well) can bind recombinant human bFGF with a linear range of 0.1-10 ng/mL. Fully biologically active when compared to standard. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Thrombopoietin (TPO), is a key regulator of megakaryocytopoiesis and thrombopoiesis. The 353 amino acid (aa) human TPO precursor is cleaved to yield the 332 aa mature protein. Mature human TPO shares approximately 70% aa sequence homology with mouse and rat TPO. TPO and its receptor (c-Mpl) are the major regulators of megakaryocyte and platelet production and serve a critical and non-redundant role in hematopoietic stem cell (HSC) biology. TPO signals through the Jak-STAT, Ras-Raf-MAPK, and PI3K pathways, and promotes survival, proliferation, and polyploidization in megakaryocytes. The proto-oncogene c- also plays an important role in many of these same processes.   Product Properties Synonyms MGDF, MGDFC-mpl ligand, MKCSF, MK-CSF, ML, MPL ligand, MPLLG, THCYT1, THPO Accession NP_000451.1 Source HEK293 Cells-derived human TPO protein, Ser 22-Gly 353 with His tag at the N-terminus. Molecular Weight Approximately 37.6 kDa. As a result of glycosylation, TPO migrates as an approximately 78.2 kDa band in SDS-PAGE under reducing conditions. AA Sequence SPAPPACDL RVLSKLLRDS HVLHSRLSQC PEVHPLPTPV LLPAVDFSLG EWKTQMEETK AQDILGAVTL LLEGVMAARG QLGPTCLSSL LGQLSGQVRL LLGALQSLLG TQLPPQGRTT AHKDPNAIFL SFQHLLRGKV RFLMLVGGST LCVRRAPPTT AVPSRTSLVL TLNELPNRTS GLLETNFTAS ARTTGSGLLK WQQGFRAKIP GLLNQTSRSL DQIPGYLNRI HELLNGTRGL FPGPSRRTLG APDISSGTSD TGSLPPNLQP GYSPSPTHPP TGQYTLFPLP PTLPTPVVQL HPLLPDPSAP TPTPTSPLLN TSYTHSQNLS QEG Tag His Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 90 % by SDS-PAGE Biological Activity Measured in a cell proliferation assay using MO7e human megakaryocytic leukemic cells. The ED50 for this effect is typically 10-60 ng/mL. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water (400 μL) to a concentration of 0.25 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Thymic stromal lymphopoietin (TSLP) is an interleukin 7 (IL-7)-like cytokine originally characterized by its ability to promote the activation of B cells and dendritic cells (DCs). Both mouse TSLP and IL-7 can co-stimulate growth of thymocytes and mature T cells, and support B lymphopoiesis in long-term cultures of fetal liver cells and bone-marrow cells. Whereas mouse IL-7 facilitates the development of B220+/IgM- pre-B cells, mouse TSLP promotes the development B220+/IgM+ B cells. Human TSLP was reported   to preferentially stimulate myeloid cells; inducing the release of T cell-attracting chemokines from monocytes and enhancing the maturation of CD11c+ dendritic cells. Thymic stromal lymphopoietin (TSLP) is a cytokine expressed by epithelial cells, including keratinocytes, and is important in allergic inflammation. Subsequent studies have shown that TSLP promotes T helper type 2 (TH2) cell responses associated with immunity to some helminth parasites and the pathogenesis of many inflammatory diseases, including atopic dermatitis and asthma. TSLP can promote TH2 cytokine-associated inflammation by directly promoting the effector functions of CD4+ TH2 cells, basophils and other granulocyte populations while simultaneously limiting the expression of DC-derived proinflammatory cytokines and promoting regulatory T cell responses in peripheral tissues.   Product Properties Synonyms thymic stromal lymphopoietin Accession Q969D9 GeneID 85480 Source E.coli-derived Human TSLP, Tys29-Gln159, with an N-terminal Met Molecular Weight Approximately 15.1 kDa. AA Sequence MYDFTNCDFE KIKAAYLSTI SKDLITYMSG    TKSTEFNNTV SCSNRPHCLT EIQSLTFNPT AGCASLAKEM FAMKTKAALA IWCPGYSETQ INATQAMKKR RKRKVTTNKC LEQVSQLQGL WRRFNRPLLK QQ Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 98% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using human IL-7Rα and human TSLP R co-transfected murine BaF3 pro-B cells is less than 0.3 ng/mL, corresponding to a specific activity of > 3.3× 106 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM PB, pH 7.4, 150 mM NaCl. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Thymosin Beta 4 is a naturally occurring peptide encoded by the TMSB4X gene located on Chr. X in humans. It is found in high concentrations in blood platelets, wound fluid and other tissues in the body. Tβ-4 is a major actin regulating peptide and the primary function is to stimulate the productions of T cells, which plays important part of the immune system. The thymosin beta-4 peptide, if used after a heart attack, might reactivate cardiac progenitor cells to repair damaged heart tissue.   Product Properties Synonyms Fx Accession P62328 GeneID 7114 Source E.coli-derived human Tβ-4 protein, Ser2-Ser44.  Molecular Weight Approximately 4.9 kDa. AA Sequence SDKPDMAEIE KFDKSKLKKT ETQEKNPLPS KETIEQEKQA GES Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97% by SDS-PAGE and HPLC analyses. Biological Activity The biological activity determined by its ability to produce a protective effect against hydrogen peroxide in primary lung fibroblasts is in a concentration range of 0.5 - 10 μg/mL. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM PB, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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CCL17, also known as thymus and activation-related chemokine (TARC), a small cytokine belonging to the C-C chemokine family. Among CC chemokine family members, CCL17 has approximately 24 - 29% amino acid sequence identity with RANTES, MIP-1 alpha, MIP-1 beta, MCP-1, MCP-2, MCP-3 and I-309. CCL17 is constitutively expressed in thymus, and at a lower level in lung, colon, and small intestine. CCL17 is also transiently expressed in phytohemagglutinin-stimulated peripheral blood mononuclear cells. CCL17 has been shown to be chemotactic for T cell lines but not monocytes or neutrophils. CCL17 was identified to be a specific functional ligand for CCR4, a receptor that is selectively expressed on T cells.   Product Properties Synonyms MGC138273, SCYA17, SCYA17MGC138271 Accession Q92583 GeneID 6361 Source E.coli-derived Human TARC/CCL17, Ala24-Ser93. Molecular Weight Approximately 8.1 kDa. AA Sequence ARGTNVGREC CLEYFKGAIP LRKLKTWYQT SEDCSRDAIV FVTVQGRAIC SDPNNKRVKN AVKYLQSLER S Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97% by SDS-PAGE and HPLC analyses. Biological Activity The biological activity determined by a chemotaxis bioassay using human T-lymphocytes is in a concentration range of 1.0-10 ng/mL. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM PB, pH 7.4, 150 mM NaCl. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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TECK is a CC chemokine, specifically expressed by thymic stromal cells, and signals through the CCR9 receptor. TECK is chemotactic towards activated macrophages, thymocytes and dendritic cells. Recombinant Human TECK is a 14.3 kDa protein containing 127 amino acid residues, including the four conserved cysteine residues present in CC chemokines.   Product Properties Synonyms TECK, CCL25, SCYA25, Ckb15 Accession O15444 GeneID 6370 Source E.coli-derived Human CCL25 protein,Glu24-Leu150. Molecular Weight Approximately 14.3 kDa. AA Sequence MQGVFEDCCL AYHYPIGWAV LRRAWTYRIQ EVSGSCNLPA AIFYLPKRHR KVCGNPKSRE VQRAMKLLDA RNKVFAKLHH NTQTFQAGPH AVKKLSSGNS KLSSSKFSNP ISSSKRNVSL LISANSGL Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97% by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The biological activity determined by a chemotaxis bioassay using human monocytes is in a concentration range of 1.0-10 ng/ml. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM PB, pH 7.4, 150 mM NaCl. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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TL-1A belongs to the TNF superfamily of ligands. It is expressed predominantly in endothelial cells, and to a lesser extent in the placenta, lung, kidney, skeletal muscle, pancreas, small intestine and colon. TL-1A inhibits endothelial cell proliferation and angiogenesis.   Product Properties Synonyms TL1A; TNF-like 1 Accession O95150 Source E.coli-derived Human TL-1A protein,Leu72-Leu251. Molecular Weight Approximately 20.5 kDa Purity > 97% by SDS-PAGE. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4, with 1% BSA. Reconstitution 1. We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile PBS, pH 7.4, with 0.1% BSA to a concentration of 0.1-1.0 mg/mL. 2. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. 3.Further dilutions should be made in PBS, which must contain carrier proteins, such as 0.1% BSA, 10% FBS, 5% HSA, 5% trehalose, one of four options.   Shipping and Storage The product should be stored at -25~-15℃ for 1 year date of receipt. 1 month, 2 ~8 °C under sterile conditions after reconstitution. 3 months, -25~-15℃ °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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TWEAKR belongs to the TNF family of transmembrane proteins, and contains a cytoplasmic "death domain", which can activate a cell's apoptotic machinery. It is expressed in the spleen, thymus, peripheral blood lymphocytes, colon, and small intestine. Signal transduction by TWEAKR can be activated by either membrane-anchored or soluble TWEAK. Recombinant Human soluble TWEAKR is a 53 amino acid polypeptide (5.6 kDa) comprising the entire extracellular domain of the full-length TWEAKR protein.   Product Properties Synonyms TNFRSF12A, FGF-inducible 14, CD266 Accession Q9NP84  GeneID  51330 Source E.coli-derived Human TWEAK Receptor/TNFRSF12A protein,Glu28-Pro80. Molecular Weight Approximately 5.6 kDa Sequence EQAPGTAPCS RGSSWSADLD KCMDCASCRA RPHSDFCLGC AAAPPAPFRL LWP Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95% by SDS-PAGE and HPLC analyses Biological Activity Fully biologically active when compared to standard. The ED50 as determined by inhibiting TWEAK-dependent proliferation of human umbilical vein endothelial cells (HUVEC) is less than 30ng/ml, corresponding to a specific activity of > 3.3 × 104 IU/mg, in the presence of 15 ng/mL of rHuTWEAK. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Transforming growth factor-beta 1 (TGF-β1) is a major pluripotential cytokine with a pronounced immunosuppressive effect. TGF-β1 is a key regulator of diverse biological processes in many tissues and cell types, its can be tumorsuppressive through the activation of the Smadmediated signaling pathway.   Product Properties Synonyms CEDLAP, DPD1, latency-associated peptide, TGF beta, TGF beta1 Uniprot No. P01137 Source HEK293-derived Human TGF-β1, Ala279-Ser390. Molecular Weight The protein has a predicted 12.8 kDa Purity > 95% as determined by SDS-PAGE. Biological Activity Measured by the (CAGA)12—luciferase reporter assay. The EC50 for this effect is 1.092 ng/mL. Endotoxin < 0.01 EU per 1μg of the protein by the LAL method. Formulation Dissolved in sterile PBS buffer. Concentration 0.5 mg/ml   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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TACI, a member of the TNF Receptor superfamily, is expressed in the small intestine, spleen, thymus, peripheral blood leukocytes, activated T cells, and resting B cells. TACI can bind to both APRIL and BAFF, stimulate the activation of transcription factors NF-κB and AP-1, and can mediate the calcineurin-dependent activation of NF-AT (nuclear-factor of activated T cells). TACI also plays a key role in the stimulation of B and T cell function. Soluble TACI inhibits APRIL-stimulated proliferation of primary B cells by blocking the binding of APRIL to the membrane-anchored TACI receptor. Recombinant Human TACI is a soluble 159 amino acid polypeptide (17.8 kDa) comprising the TNFR homologous, cysteine-rich extracellular domain of the TACI protein.   Product Properties Synonyms TACI,TNFRSF13B Accession O14836 GeneID 23495 Source E.coli-derived Human Endostatin protein,Met1-Val160,with an N-terminal Met. Molecular Weight Approximately 18.0 kDa. AA Sequence MSGLGRSRRG GRSRVDQEER FPQGLWTGVA MRSCPEEQYW DPLLGTCMSC KTICNHQSQR TCAAFCRSLS CRKEQGKFYD HLLRDCISCA SICGQHPKQC AYFCENKLRS PVNLPPELRR QRSGEVENNS DNSGRYQGLE HRGSEASPAL PGLKLSADQV Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95 % by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The biological activity is determined by its ability to block human BAFF induced T2B cell survival using a concentration range of 1.0-3.0 µg/mL. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Trefoil factor 1 belongs to the trefoil factor family that consists of three members named TFF1, TFF2 and TFF3. They are characterized by having at least one copy of the trefoil motif, a 40-amino acid domain that contains three conserved disulfides.  Mature human TFF1 shares 67% amino acid sequence identity with mouse and rat TFF1. The TFFs are stable secretory proteins expressed highly in the gastrointestinal tract (gastric mucosa). TFF1 is an essential protein for normal differentiation of the antral and pyloric gastric mucosa and functions as a stabilizer of the mucous gel overlying the gastrointestinal mucosa that provides a physical barrier against various noxious agents. TFF1 is down-regulated during the progression from gastritis to gastric dysplasia to gastric cancer, although it is up-regulated in breast and prostate cancers. TFF1 inhibits the formation of calcium oxalate crystals, and its excretion in the urine is reduced in patients with kidney stones.   Product Properties Synonyms Breast Cancer Estrogen-inducible Protein, PNR-2, Polypeptide P1.A (hP1.A), Protein pS2 Accession P04155 GeneID 7031 Source E.coli-derived human TFF1 protein, Glu25-Phe84. Molecular Weight Approximately 13.2 kDa. AA Sequence EAQTETCTVA PRERQNCGFP GVTPSQCANK GCCFDDTVRG VPWCFYPNTI DVPPEEECEF Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97 % by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a chemotaxis bioassay using human MCF-7 cells is less than 10 μg/mL, corresponding to a specific activity of > 100 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4, 150 mM NaCl. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Trefoil Factor 2 (TFF2), also known as spasmolytic peptide (SP), is one of three structurally related secreted proteins that contain trefoil domains. Trefoil factor 2 belongs to the trefoil factor family that consists of three members named TFF1, TFF2 and TFF3. They are characterized by having at least one copy of the trefoil motif, a 40-amino acid domain that contains three conserved disulfides. Mature human TFF2 shares 87% and 83% amino acid sequence identity with mouse and rat TFF2. The TFFs are stable secretory proteins expressed highly in the gastrointestinal tract (gastric mucosa). TFF2 can inhibit gastrointestinal motility and gastric acid secretion. Additionally, it functions as a structural component of gastric mucus, possibly by stabilizing glycoproteins in the mucus gel through interactions with carbohydrate side chains. Administration of TFF2 can reduce the severity of experimental colitis. TFF2 is down-regulated in many gastric cancers, although it is up-regulated in some breast cancers.   Product Properties Synonyms Spasmolysin, Spasmolytic polypeptide, SP Accession Q03403 GeneID 7032 Source E.coli-derived human TFF2 protein, Glu24-Tyr129. Molecular Weight Approximately 12.0 kDa. AA Sequence EKPSPCQCSR LSPHNRTNCG FPGITSDQCF DNGCCFDSSV TGVPWCFHPL PKQESDQCVM EVSDRRNCGY PGISPEECAS RKCCFSNFIF EVPWCFFPKS VEDCHY Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97 % by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a chemotaxis bioassay using human MCF-7 cells is less than 10 ng/mL, corresponding to a specific activity of > 1.0 × 105 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM PB, pH 7.4, 130 mM NaCl. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Trefoil Factor 3 (TFF3), also known as Intestinal Trefoil Factor (ITF) and P1.B, is one of three structurally related secreted proteins that contain trefoil domains. Trefoil factor 2 belongs to the trefoil factor family that consists of three members named TFF1, TFF2 and TFF3. They are characterized by having at least one copy of the trefoil motif, a 40-amino acid domain that contains three conserved disulfides. TFF-3 is expressed by goblet cells and in the uterus, and has also been shown to express in certain cancers, including colorectal, hepatocellular, and in biliary tumors. It involves in the maintenance and repair of the intestinal mucosa, also promotes the mobility of epithelial cells in healing processes. TFF3 up-regulation is associated with and enhances tumor cell invasion and metastasis. It supports hypoxia-induced VEGF up-regulation in tumor cells and also promotes angiogenesis in non-tumor environments. Over-expression of TFF3 in type 2 diabetic mouse liver has been shown to improve glucose tolerance and insulin sensitivity.   Product Properties Synonyms Intestinal Trefoil Factor, hITF, Polypeptide P1.B, hP1.B Accession Q07654 GeneID 7033 Source E.coli-derived human TFF3 protein, Glu36-Phe94. Molecular Weight Approximately 13.2 kDa. AA Sequence EEYVGLSANQ CAVPAKDRVD CGYPHVTPKE CNNRGCCFDS RIPGVPWCFK PLQEAECTF Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97 % by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a chemotaxis bioassay using human MCF-7 cells is less than 10 μg/mL, corresponding to a specific activity of > 100 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Human TNF-alpha is a cytokine that plays a crucial role in the inflammatory response. It is produced by various immune cells such as macrophages and T-cells and is involved in the regulation of immune cell proliferation, differentiation, and apoptosis.   Product Properties Synonyms Tumor Necrosis Factor, TNFA, TNFSF2, Cachectin, Cytotoxin, Differentiation-inducing factor, DIF Uniprot No. P01375 Source E.coli-derived human TNF-α/TNFSF2 protein, Val77-Leu233, with C-terminal His tag. Molecular Weight Approximately 18.5 kDa. Purity > 95% as determined by SDS-PAGE. Endotoxin < 0.01 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS. Reconstitution Centrifuge tubes before opening. Dissolve lyophilized protein with PBS. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Shipping and Storage The product should be stored at -25~-15℃ for 1 year from date of receipt. 2-7 days, 2 ~8 °C under sterile conditions after reconstitution. 3 months, -25~-15℃ under sterile conditions after reconstitution.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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TNF-β is a potent mediator of inflammatory and immune responses. It belongs to the TNF family of ligands, and signals through TNFR1 and TNFR2. TNF-β is produced by activated T and B lymphocytes, and has similar activities to TNF-α. Like TNF-α, TNF-β is involved in the regulation of various biological processes, including cell proliferation, differentiation, apoptosis, lipid metabolism, coagulation, and neurotransmission. TNF-β forms heterotrimers with lymphotoxin-beta, which anchors TNF-β to the cell surface. TNF-β mediates the inflammatory, immunostimulatory, and antiviral response, involves in the formation of second lymphoid organs during development, has a role in apoptosis. TNF-β is produced by lymphocytes and cytotoxic for a variety of tumor cells in vitro.   Product Properties Synonyms TNFB, TNFSF1 Uniprot No. P01374 GeneID 4049 Source E.coli-derived Human Tumor Necrosis Factor-beta protein, Leu35-Leu205. Molecular Weight Approximately 18.7 kDa. AA Sequence LPGVGLTPSA AQTARQHPKM HLAHSTLKPA AHLIGDPSKQ NSLLWRANTD RAFLQDGFSL SNNSLLVPTS GIYFVYSQVV FSGKAYSPKA TSSPLYLAHE VQLFSSQYPF HVPLLSSQKM VYPGLQEPWL HSMYHGAAFQ LTQGDQLSTH TDGIPHLVLS PSTVFFGAFA L Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 96% as determined by SDS-PAGE. Biological Activity The ED50 as determined by a cytotoxicity assay using murine L929 cells is less than 5 pg/ml, corresponding to a specific activity of > 2.0 × 108 IU/mg in the presence of actinomycin D. Fully biologically active when compared to standard. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH7.4, with 0.02% Tween-20. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Uteroglobin, also called Clara cell secretory, phospholipid binding, 10 kDa or 16 kDa protein (CCSP, CCPBP, CC10 or CC16, respectively) is a small, non-glycosylated secreted protein of the secretoglobin superfamily, (designated 1A, member 1). Its name is derived from its very high expression in the pre-implantation uterus. It is produced by the non-ciliated, non-mucous secretory cells that predominate in lung bronchioles (Clara cells), and other non-ciliated epithelia that communicate with the external environment. Expression is induced by steroid hormones such as estrogen, and enhanced by the non-steroid hormone prolactin. Uteroglobin is found in blood, urine and other body fluids. Human Uteroglobin cDNA encodes a 21 amino acid (aa) signal sequence and a 70 aa mature protein. It shares 53 - 56% aa identity with mouse, rat, bovine, canine, equine or rabbit Uteroglobin, and is active in mice. The mature protein forms a disulfide-linked head-to-tail homodimer of 16 kDa. This homodimer is thought to form a binding pocket that binds hydrophobic ligands such as phospholipids, progesterone and retinols. Sequestering of prostaglandins and leukotrienes is anti-inflammatory, while sequestering of carcinogens such as polychlorinated bisphenols is anti-tumorigenic. Other immunoregulatory activities of Uteroglobin include cell migration inhibition (by binding the chemotaxis-related formyl peptide receptor FPR2 on dendritic cells), and the inhibition of T cell differentiation to a Th2 phenotype. A single nucleotide polymorphism of Uteroglobin, A38G, confers increased risk of asthma. Transglutaminase can crosslink Uteroglobin, either to itself or to other proteins such as the adhesion molecule fibronectin. Binding of fibronectin to Uteroglobin in the kidney is thought to protect against nephropathy, while binding of the lipocalin-1 receptor has been reported to suppress cancer cell motility and invasion.   Product Properties Synonyms CC10, CCSP, UGB Uniprot No. P11684 GeneID 7356 Source E.coli-derived Human Uteroglobin, Glu22-Asn91. Molecular Weight Approximately 15.8 kDa. AA Sequence EICPSFQRVI ETLLMDTPSS YEAAMELFSP DQDMREAGAQ LKKLVDTLPQ KPRESIIKLM EKIAQSSLCN Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 98% as determined by SDS-PAGE. Biological Activity The ED50 as determined by the ability of the immobilized protein to support the adhesion of the A549 human lung carcinoma cells is less than 5.0 μg/ml, corresponding to a specific activity of > 200 IU/mg. Fully biologically active when compared to standard. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH7.4 Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Vascular endothelial growth factor 121 (VEGF121) is a protein that plays a crucial role in the growth and survival of blood vessels. It stimulates the formation of new blood vessels, a process known as angiogenesis, which is essential for normal development and tissue repair. VEGF121 has therapeutic applications for conditions such as ischemic heart disease and cancer.   Product Properties Synonyms VEGFA; vascular permeability factor; vasculotropin;V EGF-A Uniprot No. P15692-9 Source Recombinant Human VEGF121 Protein is expressed from HEK293 Cells with His tag at the C-terminal. It contains Ala27-Arg147. Molecular Weight The protein has a predicted MW of 16 kDa. And it migrates as 17-25 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation. Purity > 95% as determined by SDS-PAGE. Endotoxin <0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from 0.22 μm filtered solution in PBS (pH 7.4). Reconstitution Centrifuge tubes before opening. Dissolve lyophilized protein with sterile PBS to ensure the concentration is greater than 100 ug/mL.   Shipping and Storage The product should be stored at -25~-15℃ for 1 year from date of receipt. 2-7 days, 2 ~8 °C under sterile conditions after reconstitution. 3 months, -25~-15℃ under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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PTN was identified independently by several groups as a novel heparin-binding, developmentally regulated cytokine. Depending on the biological activities studied, this protein has variously been referred to as heparin-binding brain mitogen (HBBM), heparin-binding growth factor-8 (HBGF-8), heparin-binding neurite promoting factor, heparin-binding neurotrophic factor (HBNF),  heparin-affinity regulatory peptide (HARP), heparin-binding growth-associated molecule (HB-GAM), osteoblast-specific factor  (OSF-1), and pleiotrophin. PTN is a highly conserved protein; the amino acid sequences of human, bovine, rat, and mouse PTN share > 98% homology.PTN is a member of a family of heparin-binding proteins that share sequence, structural, and functional similarity. Other members of this family include midkine (MK), and chicken retinoic acid-induced heparin-binding protein (RI-HB), an avian homologue of MK. The expression of all these cytokines is restricted and highly regulated during development. PTN can be  used as an attachment substrate to stimulate neurite outgrowth in mixed cultures of embryonic rat, mouse or chicken brain cells.  Although both natural and recombinant human PTN have been reported to be mitogenic for fibroblasts, endothelial, and epithelial cells, the data are still highly controversial.   Product Properties   Synonyms HARP; HBBM; HB-GAM; HBGF8; HBNF Accession P21246 GeneID 5764 Source E.coli-derived human PTN, Gly33-Asp168. Molecular Weight Approximately 15.3 kDa. AA Sequence GKKEKPEKKV KKSDCGEWQW SVCVPTSGDC GLGTREGTRT GAECKQTMKT QRCKIPCNWK KQFGAECKYQ FQAWGECDLN TALKTRTGSL KRALHNAECQ KTVTISKPCG KLTKPKPQAE SKKKKKEGKK QEKMLD Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 96 % by SDS-PAGE and HPLC analyses. Biological Activity The biological activity was measured by its ability to enhance neurite outgrowth of E16-E18 rat embryonic cortical neurons, when neurons were plated on 96 well culture plates that had been pre-coated with 100 µl/well of a solution of 5-10 µg/mL rHuPTN. Fully biologically active when compared to standard. Endotoxin Less than 0.1 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom.Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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Kallikrein 3, commonly known as prostate specific antigen (PSA), is a serine protease of the human tissue Kallikrein gene family. The human tissue kallikrein (KLK) gene family contains 15 members that play important roles in cancer. Kallikrein-3, called prostate specific antigen (PSA), is a glycoprotein enzyme encoded in humans by the KLK3 gene. PSA is secreted by the epithelial cells of the prostate gland, hydrolyzes semenogelin-1 thus leading to the liquefaction of the seminal coagulum. PSA is an established tumor marker that aids in the diagnosis, staging, and follow up of prostate cancer.   Product Properties   Synonyms APS seminin, hK3, Kallikrein 3, KLK2A1, KLK3, P-30 antigen, PSA Accession P07288 GeneID 354 Source E.coli-derived human PSA/Kallikrein-3 protein, Ile25-Pro261. Molecular Weight Approximately 26.1 kDa. AA Sequence IVGGWECEKH SQPWQVLVAS RGRAVCGGVL VHPQWVLTAA HCIRNKSVIL LGRHSLFHPE DTGQVFQVSH SFPHPLYDMS LLKNRFLRPG DDSSHDLMLL RLSEPAELTD AVKVMDLPTQ EPALGTTCYA SGWGSIEPEE FLTPKKLQCV DLHVISNDVC AQVHPQKVTK FMLCAGRWTG GKSTCSGDSG GPLVCNGVLQ GITSWGSEPC ALPERPSLYT KVVHYRKWIK DTIVANP Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95 % by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The biological activity determined by a chemotaxis bioassay using human monocytes is in a concentration of 10-100 ng/ml. Endotoxin Less than 0.1 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20mM Tris-HCl, pH 8.0, 150mM NaCl, 3% trehalose Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom.Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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S100B is a member of the S100 family of proteins containing two EF-hand-type calcium-binding motifs. S100B exerts both  intracellular and extracellular functions. Intracellular S100B acts as a stimulator of cell proliferation and migration and an inhibitor of apoptosis and differentiation, which might have important implications during brain, cartilage and skeletal muscle development and repair, activation of astrocytes in the course of brain damage and neurodegenerative processes, and of cardiomyocyte remodeling after infarction, as well as in melanomagenesis and gliomagenesis. As an extracellular factor, S100B engages RAGE (receptor for advanced glycation end products) in a variety of cell types with different outcomes (i.e. beneficial or detrimental, pro-proliferative or pro-differentiative) depending on the concentration attained by the protein, the cell type and the microenvironment. This calcium binding astrocyte-specific cytokine, presents a marker of astrocytic activation and reflects CNS injury. The excellent sensitivity of S100B has enabled it to confirm the existence of subtle brain injury in patients with mild head trauma, strokes, and after successful resuscitation from cardiopulmonary arrest. Recent findings provide evidence, that S100B may decrease neuronal injury and/or contribute to repair following traumatic brain injury (TBI). Hence, S100B, far from being a negative determinant of outcome, as suggested previously in the human TBI and ischemia literature, is of potential therapeutic value that could improve outcome in patients who sustain various forms of acute brain damage.   Product Properties   Synonyms NEF Protein, Human; S100 Protein, Human; S100-B Protein, Human; S100beta Protein, Human Accession P04271 GeneID 6285 Source E.coli-derived Human S100B protein,Ser2-Glu92 Molecular Weight Approximately 10.6 kDa. AA Sequence SELEKAMVALIDVFHQYSGREGDKHKLKKSELKELINNELSHFLEEIKEQEVVDKVMETLDNDG DGECDFQEFMAFVAMVTTACHEFFEH E Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97 % by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The biological activity determined by a chemotaxis bioassay using human monocytes is in a concentration of 10-100 ng/ml. Endotoxin Less than 1 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from a 0.2 mm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom.Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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Fas and Fas Ligand (FasL) belong to the TNF superfamily, and are type I and type II transmembrane proteins, respectively. Binding of FasL to Fas triggers apoptosis in Fas-bearing cells. The mechanism of apoptosis involves recruitment of pro-caspase 8 through an adaptor molecule called FADD, followed by processing of the pro-enzyme into active forms. These active caspases then cleave various cellular substrates, leading to the eventual cell death. sFasR is capable of inhibiting FasL-induced apoptosis by acting as a decoy receptor that serves as a sink for FasL. The full length Fas (receptor) is a 319 amino acid type I transmembrane protein, which contains a 157 amino acid extracellular domain, a 17 amino acid transmembrane domain, and a 145 amino acid cytoplasmic domain. Recombinant Human soluble Fas (sFas Receptor) is a 157 amino acid polypeptide (17.6 kDa) corresponding to the TNFR-homologous cysteine-rich extracellular Fas domain. Product Properties   Synonyms TNFRSF6, CD95, Apo I, Fas Antigen Accession P25445 GeneID 355 Source E.coli-derived Human sFasR/TNFRSF6 protein,Arg17-Asn173. Molecular Weight Approximately 17.6 kDa. AA Sequence RLSSKSVNAQ VTDINSKGLE LRKTVTTVET QNLEGLHHDG QFCHKPCPPG ERKARDCTVN GDEPDCVPCQ EGKEYTDKAH FSSKCRRCRL CDEGHGLEVE INCTRTQNTK CRCKPNFFCN STVCEHCDPC TKCEHGIIKE CTLTSNTKCK EEGSRSN Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95 % by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The ED50 as determined by its ability to inhibit the cytotoxicity of Jurkat cells is between 10-15 µg/mL in the presence of 2 ng/mLof rHuFas Ligand. Endotoxin Less than 1.0 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from a 0.2 mm filtered concentrated solution in 20 mM PB, pH 7.4, 150 mM NaCl. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom.Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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TNF receptor 1 (TNF RI; also called TNF R-p55/p60 and TNFRSF1A) is a 55 kDa type I transmembrane protein member of the TNF receptor superfamily, designated TNFRSF1A. Human TNF RI is a 455 amino acid (aa) protein that contains a 21 aa signal sequence and 190 aa ECD with a PLAD (pre-ligand assembly domain) that mediates constitutive dimer/trimer formation, followed by four CRD (cysteine-rich domains), a 23 aa transmembrane domain, and a 221 aa cytoplasmic sequence that contains a neutral sphingomyelinase activation domain and a death domain. The ECD of human TNF RI shows 70%, 69%, 80%, 80%, and 73% aa identity with mouse, rat, canine, feline and porcine TNF RI, respectively; and it shows 23% aa identity with the ECD of TNF RII. Both TNF RI and TNF RII (TNFRSF1B) are widely expressed and contain four TNF-alpha trimer-binding CRD in their ECD. However, TNF RI is thought to mediate most of the cellular effects of TNF-alpha. It is essential for proper development of lymph node germinal centers and Peyer's patches, and for combating intracellular pathogens such as Listeria. TNF RI is also a receptor for TNF-beta /TNFSF1B (lymphotoxin-alpha ). TNF RI is stored in the Golgi and translocates to the cell surface following pro-inflammatory stimuli. TNF-alpha stabilizes TNF RI and induces its sequestering in lipid rafts, where it activates NF kappa B and is cleaved by ADAM-17/TACE. Product Properties   Synonyms Human sTNF RI Accession P19438 GeneID 7132 Source E.coli-derived Human sTNF RI protein,Ile22-Thr211. Molecular Weight Approximately 17.6 kDa. AA Sequence IYPSGVIGLV PHLGDREKRD SVCPQGKYIH PQNNSICCTK CHKGTYLYND CPGPGQDTDC RECESGSFTA SENHLRHCLS CSKCRKEMGQ VEISSCTVDR DTVCGCRKNQ YRHYWSENLF QCFNCSLCLN GTVHLSCQEK QNTVCTCHAG FFLRENECVS CSNCKKSLEC TKLCLPQIEN VKGTEDSGTT Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97 % by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The ED50 as determined by its ability to inhibit the TNF-alpha mediated cytotoxicity in the L-929 cells is less than 0.05 μg/mL, corresponding to a specific activity of > 2 × 10 4IU/mg in the presence of 0.25 ng/mL of rHuTNF-alpha. Endotoxin Less than 0.1 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from a 0.2 mm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom.Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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TNF RII (Tumor Necrosis Factor Receptor II), also known as TNFRSF1B, p75/p80, and CD120b, is a widely expressed receptor for membrane-associated TNF-alpha and Lymphotoxin-alpha. Its activation initiates pro-inflammatory and pro-survival responses via NFkB-dependent signaling pathways, although it may also induce apoptosis. Product Properties   Synonyms Human sTNF RII Accession P20333 GeneID 7133 Source E.coli-derived Human sTNF RI protein,Ile22-Thr211. Molecular Weight Approximately 20.0kDa. AA Sequence MPAQVAFTPY APEPGSTCRL REYYDQTAQM CCSKCSPGQH AKVFCTKTSD TVCDSCEDST YTQLWNWVPE CLSCGSRCSS DQVETQACTR EQNRICTCRP GWYCALSKQE GCRLCAPLRK CRPGFGVARP GTETSDVVCK PCAPGTFSNT TSSTDICRPH QICNVVAIPG NASMDAVCTS TSPT Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97 % by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The ED50 as determined by its ability to inhibit the TNF-α mediated cytotoxicity in the L-929 cells is less than 0.2 μg/mL, corresponding to a specific activity of > 5000 IU/mg in the presence of 0.25 ng/mL of rHuTNF-α. Endotoxin Less than 0.1 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from a 0.2 mm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom.Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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Sox2 belongs to a diverse family of structurally-related transcription factors whose primary structure contains a 79-residue DNA-binding domain, called high mobility group (HMG) box. It plays an essential role in maintaining the pluripotency of embryonic stem cells (ESC) and the determination of cell fate. Microarray analysis showed that Sox2 regulates the expression of multiple genes involved in embryonic development, including FGF-4, YES1 and ZFP206. Sox2 acts as a transcriptional activator after forming a ternary complex with Oct3/4 and a conserved non-coding DNA sequence (CNS1) located approximately 2 kb upstream of the RAX promoter. The introduction of Sox2, Oct4, Myc, and Klf4 into human dermal fibroblasts isolated from a skin biopsy of a healthy research fellow was sufficient to confer a pluripotent state upon the fibroblast genome. The reprogrammed cells thus obtained resemble ESC in morphology, gene expression, and in their capacity to form teratomas in immune-deficient mice. Sox2 and other transcription factors have been introduced into cells by DNA transfection, viral infection, or microinjection. Product Properties   Synonyms SOX2-TAT Accession P48431 GeneID 6657 Source E.coli-derived Human SOX2-TAT, Met1-Met317, with an N-terminal Met. Molecular Weight Approximately 36.0kDa. AA Sequence MYNMMETELK PPGPQQTSGG GGGNSTAAAA GGNQKNSPDRVKRPMNAFMVWSRGQRRKMA QENPKMHNSE ISKRLGAEWK LLSETEKRPF IDEAKRLRAL HMKEHPDYKYRPRRKTKTLM KKDKYTLPGG LLAPGGNSMA SGVGVGAGLG AGVNQRMDSY AHMNGWSNGS YSMMQDQLGY PQHPGLNAHG AAQMQPMHRY DVSALQYNSM TSSQTYMNGS PTYSMSYSQQ GTPGMALGSM GSVVKSEASS SPPVVTSSSH SRAPCQAGDL RDMISMYLPG AEVPEPAAPS RLHMSQHYQS GPVPGTAING TLPLSHMGGY GRKKRRQRRR Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95 % by SDS-PAGE and HPLC analyses. Biological Activity Data Not Available. Endotoxin Less than 1.0 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 2 × PBS, pH 7.4, with 5% Trehalose. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom.Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃  for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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Shh (Sonic Hedgehog protein) is a signaling molecule and a member of the Hedgehog (Hh) family. It plays a crucial role in physiological processes such as embryonic development, tissue regeneration, and cell proliferation. The Shh protein activates the Hh signaling pathway by binding to its receptor Patched (Ptch), which in turn activates the G protein-coupled receptor Smoothened (Smo). This signaling pathway is involved in the directed development of various organs and tissues during embryogenesis, including the central nervous system, limbs, and cardiovascular system. Due to the importance of Shh protein in development and tissue repair, it is also widely studied for its applications in stem cell culture, tissue engineering, and drug development. This recombinant human Shh is provided in the form of lyophilized powder, with high activity, high purity, low endotoxin, and without any additional tags. Product Properties   Synonyms HHG1, HHG-1, HLP3, HPE3, MCOPCB5 Accession Q15465 Source E.coli-derived Human shh, Cly25-Gly197, with an N-terminal Met. Molecular Weight Approximately 19.8kDa. AA Sequence IVIGPGRGFG KRRHPKKLTP LAYKQFIPNV AEKTLGASGR YEGKISRNSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDKLNALAI SVMNQWPGVK LRVTEGWDED GHHSEE SLHY EGRAVDITTS DRDRSKYGML ARLAVEAGFD WVYYESKAHI HCSVKAENSVAAKSGG Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 98 % by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by inducing alkaline phosphatase production of murine C3H/10T1/2 cells is less than 1 μg/mL, corresponding to a specific activity of > 1.0 × 103 IU/mg. Fully biologically active when compared to standard. Endotoxin Less than 1.0 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM PB, pH 7.4, 150 mM NaCl. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom.Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at-25~-15℃  for 1 year. 7 days, 2 to 8 °C under sterile conditions after reconstitution.  3 months,-85~-65℃ under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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This gene encodes insulin, a peptide hormone that plays a vital role in the regulation of carbohydrate and lipid metabolism. After removal of the precursor signal peptide, proinsulin is post-translationally cleaved into three peptides: the B chain and A chain peptides, which are covalently linked via two disulfide bonds to form insulin, and C-peptide. Binding of insulin to the insulin receptor (INSR) stimulates glucose uptake. A multitude of mutant alleles with phenotypic effects have been identified. There is a read-through gene, INS-IGF2, which overlaps with this gene at the 5' region and with the IGF2 gene at the 3' region. Alternative splicing results in multiple transcript variants. Product Properties   Synonyms Human Proinsulin C-Peptide Analogue, IDDM Protein, Human; IDDM1 Protein, Human Accession P01308 GeneID 3630 Source E.coli-derived human Proinsulin C-Peptide Analogue protein,Arg55-Arg89 Molecular Weight Approximately 3.6 kDa. AA Sequence RREAEDLQVG QVELGGGPGA GSLQPLALEG SLQKR Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95 % by SDS-PAGE and HPLC analyses. Biological Activity Data Not Available. Endotoxin Less than 0.1 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom.Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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Rb encoded by the RB1 gene in humans, is expressed by retina and belongs to the etinoblastoma-associated protein family. The hole protein consists of 928 a.a. and the rHuRb fragment occupies sequence of 792-929 a.a.. Rb is a key regulator of entry into cell division that acts as a tumor suppressor. It has many functions, for example, promotes G0-G1 transition when phosphorylated by CDK3/cyclin-C, and acts as a transcription repressor of E2F1 target genes and so on. The rHuRb is the region that rich of modified residue like phosphothreonine and N6-acetyllysine. Product Properties   Synonyms p105-Rb, pRb, pp110 Accession Q59HH0 GeneID 4595173 Source E.coli-derived human Rb137 protein, Phe792-Lys928. Molecular Weight Approximately 16.5 kDa. AA Sequence MASFPSSPLR IPGGNIYISP LKSPYKISEG LPTPTKMTPR SRILVSIGES FGTSEKFQKI NQMVCNSDRV LKRSAEGSNP PKPLKKLRFD IEGSDEADGS KHLPGESKFQ QKLAEMTSTR TRMQKQKMND SMDTSNKEEK HHHHHH Tag C-His Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95 % by SDS-PAGE and HPLC analyses. Biological Activity Data Not Available. Endotoxin Less than 1.0 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom.Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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Secreted protein acidic and rich in cysteine (SPARC), also named as osteonectin or BM-40, is an acronym for “secreted protein, acidic and rich in cysteine”. Mature human SPARC shows 92%, 92%, 97%, 99%, 96% and 85% aa identity with mouse, rat, canine, bovine, porcine and chick SPARC. SPARC is the founding member of a family of secreted matricellular proteins with similar domain structure. It is produced by fibroblasts, capillary endothelial cells, platelets and macrophages, especially in areas of tissue morphogenesis and remodeling. SPARC is required for the collagen in bone to become calcified but is also involved in extracellular matrix synthesis and promotion of changes to cell shape. The gene product has been associated with tumor suppression but has also been correlated with metastasis based on changes to cell shape which can promote tumor cell invasion.   Product Properties   Synonyms Basement-membrane Protein 40, BM-40, Osteonectin, ON, SPARC Accession P09486 GeneID 6678 Source E.coli-derived human SPARC protein, Ala18-Asp1303. Molecular Weight Approximately 32.7 kDa. AA Sequence APQQEALPDE TEVVEETVAE VTEVSVGANP VQVEVGEFDD GAEETEEEVV AENPCQNHHC KHGKVCELDE NNTPMCVCQD PTSCPAPIGE FEKVCSNDNK TFDSSCHFFA TKCTLEGTKK GHKLHLDYIG PCKYIPPCLD SELTEFPLRM RDWLKNVLVT LYERDEDNNL LTEKQKLRVK KIHENEKRLE AGDHPVELLA RDFEKNYNMY IFPVHWQFGQ LDQHPIDGYL SHTELAPLRA PLIPMEHCTT RFFETCDLDN DKYIALDEWA GCFGIKQKDI DKDLVI Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 99 % by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by its ability to inhibit the cell growth of Mv1Lu mink lung epithelial cells is less than 3.0 μg/mL, corresponding to a specific activity of > 333 IU/mg. Fully biologically active when compared to standard. Endotoxin Less than 0.1 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom.Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Storage   The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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SCF, also known as stem cell factor or kit ligand, is a cytokine that plays a critical role in the survival, proliferation, and differentiation of hematopoietic stem cells and early progenitor cells. SCF is primarily produced by bone marrow stromal cells and functions by binding to the c-kit receptor on the surface of hematopoietic cells. Dysregulation of SCF signaling has been implicated in various types of cancer and hematological disorders.   Product Properties   Synonyms KITLG; FPH2; KL-1; Kitl; MGF; SF; SHEP7; KL Accession P21583-1 Source Recombinant Human SCF Protein is expressed from E.coli without tag. It contains Glu26-Ala189 Molecular Weight Approximately 18.45 kDa. Tag None Purity > 95% by SDS-PAGE and HPLC analyses. Endotoxin Less than 1.0 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from 0.22 μm filtered solution in PBS (pH 7.4). Normally 8% trehalose is added as protectant before lyophilization. Reconstitution Centrifuge the tube before opening, Reconstituting to a concentration more than 100 μg/ml is recommended. Dissolve the lyophilized protein in distilled water.   Storage   The product should be stored at -25~-15℃ for 1 year from date of receipt. 2-7 days, 2 ~8 °C under sterile conditions after reconstitution. 3 -6 months, -85~-65℃ under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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CXCL12, also known as SDF-1, is a small (8 kDa) cytokine highly conserved chemotactic cytokine belonging to the large family of CXC chemokines. SDF-1 alpha and SDF-1 beta are the first cytokines initially identified using the signal sequence trap cloning strategy from a mouse bone-marrow stromal cell line. They are identical except for the four residues present in the C-terminus of SDF1β but absent from SDF1α. CXCL12 binds primarily to CXC receptor 4. The binding of CXCL12 to CXCR4 induces intracellular signaling through several divergent pathways initiating signals related to chemotaxis, cell survival and/or proliferation, increase in intracellular calcium, and gene transcription. The CXCL12/CXCR4 axis is involved in tumor progression, angiogenesis, metastasis, and survival. CXCL12 also can influence lymphopoiesis and regulate patterning and cell number of neural progenitor.   Product Properties   Synonyms SDF-1 alpha, hSDF-1 alpha, IRH, hIRH, PBSF Accession P48061 GeneID 6387 Source E.coli-derived Human SDF-1α/CXCL12α, Lys22-Lys89 Molecular Weight Approximately 8.0 kDa. AA Sequence KPVSLSYRCP CRFFESHVAR ANVKHLKILN TPNCALQIVA RLKNNNRQVC IDPKLKWIQE YLEKALNK Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97 % by SDS-PAGE and HPLC analyses. Biological Activity The biological activity determined by a chemotaxis bioassay using PHA and rHuIL-2 activated human peripheral blood T-lymphocytes is in a concentration range of 20-80 ng/mL. Fully biologically active when compared to standard. Endotoxin Less than 1.0 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM PB pH 7.0, 130 mM NaCl. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom.Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Storage The products are shipped with ice pack and can be stored at -20 ℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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CXCL12, also known as SDF-1, is a heparin-binding member of the CXC (or alpha-) family of chemokines. SDF-1 alpha and SDF-1 beta are the first cytokines initially identified using the signal sequence trap cloning strategy from a mouse bone-marrow stromal cell line. These proteins were subsequently also cloned from a human stromal cell line. CXCL12β is synthesized as a 93 amino acid (aa) precursor that contains a 21 aa signal sequence and a 72 aa mature region. The mature molecule exhibits a typical three antiparallel beta -strand chemokine-like fold. There are no potential N-linked glycosylation sites.The C-terminus is likely associated with heparin binding . SDF-1 beta circulates and undergoes proteolytic processing. CD26 will remove the first two N-terminal amino acids, possibly creating a reduced-activity chemokine. On the cell surface, the receptor for this chemokine is CXCR4 and syndecan4. Among its many functions, CXCL12 is known to influence lymphopoiesis, regulate patterning and cell number of neural progenitors, and promote angiogenesis. It also enhances the survival of myeloid progenitor cells.   Product Properties   Synonyms hSDF-1 beta, IRH, hIRH, PBSF Accession P48061 GeneID 6387 Source E.coli-derived Human SDF-1β/CXCL12β, Lys22-Met93. Molecular Weight Approximately 8.5 kDa. AA Sequence KPVSLSYRCP CRFFESHVAR ANVKHLKILN TPNCALQIVA RLKNNNRQVC IDPKLKWIQE YLEKALNKRF KM Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97 % by SDS-PAGE and HPLC analyses. Biological Activity The biological activity determined by a chemotaxis bioassay using PHA and rHuIL-2 activated human peripheral blood T-lymphocytes is in a concentration range of 20-80 ng/mL. Fully biologically active when compared to standard. Endotoxin Less than 1.0 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom.Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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Human CXCL12 is expressed as five isoforms that differ only in the C-terminal tail. The gamma isoform of CXCL12, also known as SDF-1 gamma, is a 12 kDa, heparin-binding member of the CXC (or alpha) family of chemokines ,Mature SDF-1 molecules are not glycosylated and exhibit a typical three antiparallel beta -strand chemokine-like fold. N-terminal aa 1 - 8 form a receptor binding site, while aa 1 and 2 (Lys- Pro) are involved in receptor activation. All SDF-1 isoforms can undergo proteolytic processing of the first two N-terminal amino acids by CD26, which is thought to create a reduced- activity chemokine. Human SDF-1 gamma is synthesized as a 119 amino acid (aa) precursor that contains a 21 aa signal sequence and a 98 aa mature region. Mature human SDF-1 gamma shares 99%, 97% and 98% aa identity with mouse, rat, and equine SDF-1 gamma, respectively. The unique C-terminal 26 aa of SDF-1 gamma are highly charged, including four BBXB (where B = basic and X = any aa) motifs, while the most prevalent form, SDF-1 alpha, has 4 unique C-terminal aa and binds heparin via the shared BBXB site more N-terminally located . The SDF- 1 gamma C-terminus binds heparin in secreted SDF-1 gamma, or targets the isoform to the nucleolus in the absence of a signal sequence. SDF-1 isoforms interact with CXCR4 and CXCR7 receptors on the cell surface, and can also bind syndecan-4.   Product Properties   Synonyms CXCL12γ Accession P48061 GeneID 6387 Source E.coli-derived Human CXCL12γ protein,Gly21-Asn119. Molecular Weight Approximately 11.6 kDa. AA Sequence GKPVSLSYRC PCRFFESHVA RANVKHLKIL NTPNCALQIV ARLKNNNRQV CIDPKLKWIQ EYLEKALNKG RREEKVGKKE KIGKKKRQKK RKAAQKRKN Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 96 % by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The biological activity determined by a chemotaxis bioassay using PHA and rHuIL-2 activated human peripheral blood T-lymphocytes is in a concentration range of 30-100 ng/mL. Endotoxin Less than 0.1 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM PB, pH 7.4, 150 mM NaCl. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom.Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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Syndecan-4, previously known as amphiglycan or ryudocan, is a member of the syndecan family of Type 1 transmembrane proteins capable of carrying heparan sulfate (HS) and chondroitin sulfate glycosaminoglycans. Human Syndecan-4 ECD shares approximately 79%, 78% and 81% aa identity with mouse, rat and porcine Syndecan-4 ECD, respectively. Syndecans are the best-characterized plasma membrane proteoglycans with two conserved cytoplasmic domains and divergent extracellular portions, except for HS attachment sites. SYND4 is the most similar to SYND2, but is more universally expressed and is found in virtually every cell type. Expression can be upregulated by TGFβ2 and in response to mechanical stress in smooth muscle, wound healing, arterial injury or acute myocardial infarction, probably in response to at least one inflammatory mediator. SYND4 has more widespread distribution than other syndecans and it is the only syndecan that has been found consistently in focal adhesions.   Product Properties   Synonyms Amphiglycan, MGC22217, Ryudocan, SDC4, syndecan 4, Syndecan4 Accession P31431 GeneID 6385 Source E.coli-derived human SYND4 protein,Glu19-Glu145. Molecular Weight Approximately 13.9 kDa. AA Sequence ESIRETEVID PQDLLEGRYF SGALPDDEDV VGPGQESDDF ELSGSGDLDD LEDSMIGPEV VHPLVPLDNH IPERAGSGSQ VPTEPKKLEE NEVIPKRISP VEESEDVSNK VSMSSTVQGS NIFERTE Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95 % by SDS-PAGE and HPLC analyses. Biological Activity The specific activity is determined by binding ability in a functional ELISA. Immobilized recombinant human SYND4 at 500 ng/mL (100 μl/well) can bind recombinant human bFGF with a linear range of 0.1-10 ng/mL. Fully biologically active when compared to standard. Endotoxin Less than 0.1 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom.Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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RANTES is a CC chemokine that can signal through the CCR1, CCR3, CCR5 and US28 (cytomegalovirus receptor) receptors. It is a chemoattractant towards monocytes, memory T cells (CD4+/CD45RO), basophils, and eosinophils. RANTES also has the capability to inhibit certain strains of HIV-1, HIV-2 and simian immunodeficiency virus (SIV). Recombinant Human RANTES is a 7.8 kDa protein containing 68 amino acid residues, including the four highly conserved cysteine residues present in the CC chemokines.   Product Properties   Synonyms SIS-delta, Small-inducible cytokine A5, T-cell-specific protein RANTES Accession P13501 GeneID 6352 Source E.coli-derived Human CCL5 protein,Ser24-Ser91. Molecular Weight Approximately 7.8 kDa. AA Sequence SPYSSDTTPC CFAYIARPLP RAHIKEYFYT SGKCSNPAVV FVTRKNRQVC ANPEKKWVRE YINSLEMS Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 98 % by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The biological activity determined by a chemotaxis bioassay using human peripheral blood monocytes is in a concentration range of 1.0-10 ng/mL. Endotoxin Less than 0.1 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20mM PB, pH 7.4, 100 mM NaCl. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom.Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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CD40 Ligand, also known as TNFSF, a type II membrane protein with homology to TNF, is transiently expressed on activated T cells and known to be important for B cell Ig production and for activation and differentiation of monocytes and dendritic cells. Mature human CD40 Ligand consists of a 22 amino acid (aa) cytoplasmic domain, a transmembrane segment, and an 215 aa extracellular region . It is primarily expressed on activated CD4+ T lymphocytes, and also found in other types of cells, like NK cells, mast cells, basophils and eosinophils. In total CD40 ligand has three binding partners: CD40, α5β1 integrin and αIIbβ3. CD40 Ligand dysregulation on T cells and antigen presenting cells contributes to the immune deficiency associated with HIV infection and AIDS. CD40 ligation by CD40 Ligand promotes B cell activation and T cell-dependent humoral responses.   Product Properties   Synonyms CD154 antigen, CD154, CD40 antigen ligand, CD40 Ligand, gp39, HIGM1, T-B cell-activating molecule, T-BAM, TNFSF5, TNFSF5IMD3, TRAP Accession P29965 GeneID 959 Source E.coli-derived human sCD40L protein, Met113-Leu261. Molecular Weight Approximately 16.3 kDa. AA Sequence MQKGDQNPQI AAHVISEASS KTTSVLQWAE KGYYTMSNNL VTLENGKQLT VKRQGLYYIY AQVTFCSNRE ASSQAPFIAS LWLKSPGRFE RILLRAANTH SSAKPCGQQS IHLGGVFELQ PGASVFVNVT DPSQVSHGTG FTSFGLLKL Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95 % by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by the dose-dependent stimulation of IL-8 production by human PBMC is less than 5-10 ng/mL. Fully biologically active when compared to standard. Endotoxin Less than 1.0 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20mM PBS, pH 7.0. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom.Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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TRAIL Receptor-1/DR4 and TRAIL Receptor-2/DR5 belong to the TNFR superfamily of transmembrane proteins, and contain a cytoplasmic "death domain," which can activate the cell's apoptotic machinery. These receptors are activated by binding to either membrane-anchored or soluble TRAIL/Apo2L. The DR4 and DR5 receptors are both produced as type I transmembrane proteins, which contain an extracellular domain, a transmembrane domain, and a cytoplasmic domain. The recombinant soluble forms of DR4 and DR5 consist of the TNFR-homologous, cysteine-rich portion of their respective extracellular domains. Recombinant Human soluble TRAIL Receptor-2/DR5 is a 14.9 kDa protein (133 amino acid residues) consisting of the TNFR-homologous, cysteine-rich portion of the extracellular domain.   Product Properties   Synonyms soluble TRAIL Receptor-2, DR5, TNFRSF10B, KILER, TRICK2A, TRICKB Accession O14763 GeneID 8795 Source E.coli-derived Human soluble TRAIL Receptor-2 protein,Glu52-Ser183. Molecular Weight Approximately 14.8 kDa. AA Sequence ESALITQQDL APQQRAAPQQ KRSSPSEGLC PPGHHISEDG RDCISCKYGQ DYSTHWNDLL FCLRCTRCDS GEVELSPCTT TRNTVCQCEE GTFREEDSPE MCRKCRTGCP RGMVKVGDCT PWSDIECVHK ES Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97 % by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. rHusTRAIL-R2 reduced the production of LPS-induced TNF by its ability to neutralize endogenous TRAIL in fresh human PBMC. In this assay, endogenous TRAIL is induced during a 24 hour exposure to LPS (10 ng/mL) but in the presence of rHusTRAIL-R2, TRAIL-induced TNF is suppressed. Endotoxin Less than 1.0 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20mM PBS, pH 7.0. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom.Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Storage The products are shipped with ice pack and can be stored at -20℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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RANKL and RANK are members of the TNF superfamily of ligands and receptors that play an important role in the regulation of specific immunity and bone turnover. RANK (receptor) was originally identified as a dendritic cell-membrane protein, which, by interacting with RANKL, augments the ability of dendritic cells. These dendritic cells then stimulate naïve T-cell proliferation in a mixed lymphocyte reaction, promote the survival of RANK+ T-cells, and regulate T-cell-dependent immune response. RANKL, which is expressed in a variety of cells, including osteoblasts, fibroblasts, activated T-cells and bone marrow stromal cells, is also capable of interacting with a decoy receptor called OPG. Binding of soluble OPG to sRANKL inhibits osteoclastogenesis by interrupting the signaling between stromal cells and osteoclastic progenitor cells, thereby leading to excess accumulation of bone and cartilage.   Product Properties   Synonyms soluble Receptor Activator of NF-κB Ligand, TNFSF11, TRANCE (TNF-related activation-induced cytokine), OPGL, ODF Accession O14788 Source HEK293 Cells-derived human sRANKL protein, Gly64-Asp24 Molecular Weight Approximately 20.5 kDa. AA Sequence VALFFYF RAQMDPNRIS EDGTHCIYRI LRLHENADFQ DTTLESQDTK LIPDSCRRIK QAFQGAVQKE LQHIVGSQHI RAEKAMVDGS WLDLAKRSKL EAQPFAHLTI NATDIPSGSH KVSLSSWYHD RGWAKISNMT FSNGKLIVNQ DGFYYLYANI CFRHHETSGD LATEYLQLMV YVTKT Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 85 % by SDS-PAGE  analyses. Biological Activity 1. Immobilized human TNFSF11 at 2 μg/ml (100 μL/well) can bind human Osteoprotegerin hFc, the EC50 of human Osteoprotegerin hFc is 5-40 ng/mL. 2. The bioactivity of hRANKL was determined by measuring the ability of hRANKL to induce TRAP activity in Raw 264.7 cells. The ED50 for this effect is typically 1.5-7.5 ng/mL. Endotoxin Less than 1.0 EU/μg of the protein as determined by LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom.Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only.

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IL-28B (also named interferon-lambda 3, IFN-lambda 3), IL-28A (IFN-lambda 2) and IL-29 (IFN-lambda 1) are type III interferons that are class II cytokine receptor ligands. They are distantly related to members of the IL-10 family and type I IFN family. Human IL-28B cDNA encodes a 200 amino acid (aa) protein with a 25 aa signal peptide and a 175 aa mature protein that lacks N-glycosylation sites. Mature human IL-28B shares 64% and 75% aa sequence identity with mouse and canine IL-28B, respectively, and is active across species. Human IL-28B shares 94% and 69% aa identity with human IL-28A and IL- 29, respectively. Type III interferons are widely expressed, but are mainly produced by antigen presenting cells in response to viruses  and double-stranded RNA that interact with Toll-like receptors or RIG-1 family helicases. They signal through a widely expressed receptor that is a heterodimer of the IL-10 receptor beta (IL-10 R beta ) and IL-28 receptor alpha (IL-28 R alpha ; also called IFN-lambda R1). Interaction of either type I or type III IFNs with their receptors activates similar pathways, including JAK tyrosine kinase activation, STAT phosphorylation and formation of the IFN-stimulated regulatory factor 3 (ISGF-3) transcription factor complex. Both type  I and III IFNs induce anti- viral activity and up- regulate MHC class I antigen expression. Cell lines responsive to type III IFNs are also responsive to type I IFNs, but in general, higher concentrations of type III IFNs are needed for similar in vitro responses. In vivo, however, type III IFNs enhance levels of IFN-gamma in serum, suggesting that the robust anti-viral activity of type III IFNs may  stem in part from activation of the immune system. Anti-proliferative and antitumor activity in vivo has also been shown for type III IFNs.   Product Properties Synonyms Interleukin 28B；Interferon lambda-3；IFN-lambda-3；Interleukin-28B Accession Q8CGK6 GeneID 338374 Source E.coli-derived mouse Interferon-lambda3/Interleukin-28B protein, Asp20-Val193 Molecular Weight Approximately 19.6 kDa. AA Sequence DPVPRATRLP VEAKDCHIAQ FKSLSPKELQ AFKKAKGAIE KRLLEKDMRC SSHLISRAWD LKQLQVQERP KALQAEVALT LKVWENINDS ALTTILGQPL HTLSHIHSQL QTCTQLQATA EPKPPSRRLS RWLHRLQEAQ SKETPGCLED SVTSNLFQLL LRDLKCVASG DQCV Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 98% by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The ED50 as determined by an anti-viral assay using human HepG2 cells infected with encephalomyocarditis is less than 30 ng/ml, corresponding to a specific activity of > 3.3 × 104 IU/mg Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 1 × PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Interleukin-1 alpha (IL1a) is also known as IL-1A, IL1,and is a cytokine of the interleukin-1 family. Among various species, the amino acid sequence of mature IL-1 alpha is conserved 60% to 70% and human IL-1 has been found to be biologically active on murine cell lines. It possesses metabolic, physiological, haematopoietic activities, and plays one of the central roles in the regulation of the immune responses. IL-1 is a major immunoregulatory/proinflammatory cytokine which also affects fibroblast proliferation and function and therefore it was of interest to investigate whether its constitutive expression influences the in vivo tumorigenic potential of transformed fibroblastoid cell lines.   Product Properties Synonyms Interleukin-1 alpha, IL-1α, BAF, IL-1F1, LAF, LEM, preinterleukin 1 alpha, pro-interleukin-1-alpha Accession Q3U0Y6 GeneID 16175 Source E.coli-derived mouse IL-1alpha protein, Ser115-Ala270. Molecular Weight Approximately 17.9 kDa. AA Sequence SAPYTYQSDL RYKLMKLVRQ KFVMNDSLNQ TIYQDVDKHY LSTTWLNDLQ QEVKFDMYAY SSGGDDSKYP VTLKISDSQL FVSAQGEDQP VLLKELPETP KLITGSETDL IFFWKSINSK NYFTSAAYPE LFIATKEQSR VHLARGLPSM TDFQIS Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using murine D10S cells is less than 2 pg/mL, corresponding to a specific activity of > 5.0 × 108 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 1 × PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Interleukin-1 beta (IL-1β) is a pro inflammatory cytokine, which is secreted by immune cells to trigger inflammation and this has been found profoundly in the lesions caused by Leishmania pathogens. IL-1 is a name that designates two pleiotropic cytokines, IL-1 alpha (IL-1F1) and IL-1 beta (IL-1F2), which are the products of distinct genes. IL-1 alpha and IL-1 beta are structurally related polypeptides that share approximately 21% amino acid (aa) identity in human. Both IL-1α and IL-1β binds to the same receptor and has similar but not identical biological properties; The mature human IL1β shares 96% amino acid sequence identity with rhesus and 67% -78% with canine, mouse and rat IL-1β.IL-1β, are known to modulate effects of neurotoxic neurotransmitters discharged during excitation or inflammation in the central nervous system (CNS).   Product Properties Synonyms Interleukin-1 beta, IL-1β, IL-1, IL1B, IL-1b, IL1-BETA, IL-1F2, IL1F2IL-1 beta, interleukin-1 beta, preinterleukin 1 beta, pro-interleukin-1-beta. Accession P10749 GeneID 16176 Source E.coli-derived human IL-1β protein, Vla118-Ser269. Molecular Weight Approximately 17.5 kDa. AA Sequence VPIRQLHYRL RDEQQKSLVL SDPYELKALH LNGQNINQQV IFSMSFVQGE PSNDKIPVAL GLKGKNLYLS CVMKDGTPTL QLESVDPKQY PKKKMEKRFV FNKIEVKSKV EFESAEFPNW YISTSQAEHK PVFLGNNSGQ DIIDFTMESV SS Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 96% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using murine D10S cells is less than 2 pg/mL, corresponding to a specific activity of > 5.0 × 108 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 1 × PBS, pH 7.4, with 5% trehalose, 0.02% Tween-20. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20 ℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Interleukin-10 (IL-10), also known as cytokine synthesis inhibitory factor (CSIF), is the charter member of the IL-10 family of α-helical cytokines that also includes IL-19, IL-20, IL-22, IL-24, and IL-26/AK155. IL-10 is a 178 amino acid molecule that contains two intrachain disulfide bridges and is expressed as a 36 kDa noncovalently associated homodimer. Mature human IL- 10 shares 72%- 86% amino acid sequence identity with bovine, canine, equine, feline, mouse, ovine, porcine, and rat IL- 10. IL-10, a cytokine produced by CD4+ T lymphocytes belonging to the Th-2 subset, has previously been shown to inhibit the synthesis of IFN-gamma by both T cells and NK cells.The anti-inflammatory actions of IL-10 may be therapeutically useful either directly or through modulation of HO-1 activity.   Product Properties Synonyms Interleukin-10, IL-10, Cytokine synthesis inhibitory factor, IL10A, TGIF, CSIF Accession P18893 GeneID 16153 Source E.coli-derived mouse IL-10 protein, Ser19-Ser178. Molecular Weight Approximately 18.7 kDa. AA Sequence SRGQYSREDN NCTHFPVGQS HMLLELRTAF SQVKTFFQTK DQLDNILLTD SLMQDFKGYL GCQALSEMIQ FYLVEVMPQA EKHGPEIKEH LNSLGEKLKT LRMRLRRCHR FLPCENKSKA VEQVKSDFNK LQDQGVYKAM NEFDIFINCI EAYMMIKMKS Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using murine MC/9-2 cells is less than 1 ng/mL, corresponding to a specific activity of > 1.0 × 106 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 1 × PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in 10 mM HCl to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20 ℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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IL-11 is a pleiotropic cytokine in the IL-6 family, which also includes LIF, CNTF, Oncostatin M, Cardiotrophin-1, IL-27 and IL-31. IL11 is also known under the names adipogenesis inhibitory factor (AGIF) and oprelvekin.The mouse IL-11 cDNA encodes a 199 amino acid (aa) precursor, which generates a 178 aa, 19 kDa mature unglycosylated protein. It is found in the plasma mainly during inflammation, and is considered to be primarily anti- inflammatory. It stimulates hematopoiesis and thrombopoiesis, regulates macrophage differentiation, and confers mucosal protection in the intestine. It has also been found to enhance T cell polarization toward Th2, promote B cell IgG production, increase osteoclast bone absorption, protect endothelial cells from oxidative stress, and regulate epithelial proliferation and apoptosis. IL-11 synergizes with several other cytokines to produce these effects, and its effects overlap with those of IL-6. IL-11 stimulates the growth of certain lymphocytes and, in the murine model, stimulates an increase in the cortical thickness and strength of long bones. As a signaling molecule, IL-11 has a variety of functions associated with its receptor interleukin 11 receptor alpha; such functions include placentation and to some extent of decidualization.   Product Properties Synonyms AGIF Accession P47873 GeneID 16156 Source E.coli-derived Mouse IL-11, Pro22-Leut199, with an N-terminal Met. Molecular Weight Approximately 19.1 kDa. AA Sequence MPGPPAGSPR VSSDPRADLD SAVLLTRSLL ADTRQLAAQM RDKFPADGDH SLDSLPTLAM SAGTLGSLQL PGVLTRLRVD LMSYLRHVQW LRRAGGPSLK TLEPELGALQ ARLERLLRRL QLLMSRLALP QAAPDQPVIP LGPPASAWGS IRAAHAILGG LHLTLDWAVR GLLLLKTRL Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using murine T11 cells is less than 2 ng/mL, corresponding to a specific activity of > 5.0 × 105 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 1 × PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20 ℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Interleukin-13 (IL-13) was first recognized for its effects on B cells and monocytes, where it upregulated class II expression, promoted IgE class switching and inhibited inflammatory cytokine production. IL-13 is a monomeric 17 kDa immunoregulatory cytokine that plays a key role in the pathogenesis of allergy, cancer, and tissue fibrosis. Mature human IL-13 shares approximately 58% amino acid sequence identity with mouse and rat IL-13. It has become evident that IL-13 is a key mediator in the pathogenesis of allergic inflammation, and IL-13 is key proinflammatory cytokines in asthma. The cytokines interleukin IL-13 have pleiotropic effects on a variety of cell types and impact both pathologic changes and tissue remodeling.   Product Properties Synonyms BHR1interleukin-13, IL13, interleukin 13, MGC116786, NC30, P600 Accession P20109 GeneID 16163 Source E.coli-derived Mouse IL-13, Pro22-Phe131, with an N-terminal Met. Molecular Weight Approximately 12.3 kDa. AA Sequence MPVPRSVSLP LTLKELIEEL SNITQDQTPL CNGSMVWSVD LAAGGFCVAL DSLTNISNCN AIYRTQRILH GLCNRKAPTT VSSLPDTKIE VAHFITKLLS YTKQLFRHGP F Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using human TF-1 cells is less than 4 ng/mL, corresponding to a specific activity of > 2.5 × 105 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 1 × PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20 ℃ for 1 year. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 °C under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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