Cytokines

Interleukin-8 (IL-8) is encoded by the IL8 gene and produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles. There are many receptors capable to bind IL-8, the most affinity to IL-8 are receptors CXCR1, and CXCR2. As a member of the CXC chemokine family, function of IL-8 is the induction of chemotaxis in its target cells, like neutrophil granulocytes, basophils, and T-cells. IL-8 (77a.a.) has a 5-10 fold higher activity on neutrophil activation, compared to IL-8 (77a.a.). IL-8 is often associated with inflammation, it has been cited as a proinflammatory mediator in gingivitis and psoriasis.   Product Properties Synonyms CXCL 8, Emoctakin, GCP-1, MDNCF, MONAP, NAP-1, Protein 3-10C, T-cell chemotactic factor Accession P10145 GeneID 3576 Source E.coli-derived human IL-8 protein, Ala23-Ser99 Molecular Weight Approximately 8.9 kDa. AA Sequence AVLPRSAKEL RCQCIKTYSK PFHPKFIKEL RVIESGPHCA NTEIIVKLSD GRELCLDPKE NWVQRVVEKF LKRAEN 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 ED50 as determined by a chemotaxis bioassay using human CXCR2 transfected mouse BaF3 cells 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 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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CXCL11, also known as I-TAC, SCYB9B, H174 and beta -R1, is a non-ELR CXC chemokine. CXCL11 cDNA encodes a 94 amino acid (aa) residue precursor protein with a 21 aa residue putative signal sequence, which is cleaved to form the mature 73 aa residue protein. CXCL11 shares 36% and 37% amino acid sequence homology with IP-10 and MIG (two other known human non-ELR CXC chemokines), respectively. CXCL11 is expressed at low levels in normal tissues including thymus, spleen and pancreas. The expression of CXCL11 mRNA is radically up regulated in IFN-gamma and IL-1 stimulated astrocytes. Moderate increase in expression is also observed in stimulated monocytes. CXCL11 has potent chemoattractant activity for IL-2 activated T cells and transfected cell lines expressing CXCR3, but not freshly isolated T cells, neutrophils or monocytes.   Product Properties Synonyms Beta-R1, H174, IP-9, Small-inducible Cytokine B1 Accession O14625 GeneID 6373 Source E.coli-derived Human CXCL11,Phe22-Phe94 Molecular Weight Approximately 8.3 kD AA Sequence FPMFKRGRCL CIGPGVKAVK VADIEKASIM YPSNNCDKIE VIITLKENKG QRCLNPKSKQ ARLIIKKVER KNF 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 IL-2 activated human T-lymphocytes is in a concentration range of 0.1-10 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 20 mM 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.   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 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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Fibroblast growth factor 7 (FGF-7), also known as Keratinocyte Growth Factor (KGF), is a member of the fibroblast growth factor (FGF) family. It plays an important role in the regulation of embryonic development, cell proliferation, and cell differentiation. It is essential for normal branching morphogenesis and is an active growth factor for keratinocytes. It may be the main paracrine factor for the proliferation of normal epithelial cells. The activity of recombinant KGF overexpressed in E. coli is about 10 times that of the natural protein, which may be related to the lack of glycosylation of recombinant KGF. The 122-132AA segment of KGF is the specific binding site for the KGF receptor. KGF is secreted by various sources of mesenchymal cells and has a strong affinity for heparin. Its receptor, KGFR, belongs to the family of protein tyrosine kinase receptors and is mainly distributed in epithelial cells. After KGF specifically binds to the receptor KGFR on the target cell membrane, it promotes the autophosphorylation of the receptor, thereby initiating a series of intracellular signaling cascades and playing various biological functions: participating in the development of tissues and organs, promoting cell proliferation, and tissue damage repair. This product is a recombinant protein prepared by the E. coli prokaryotic expression system, and is made through steps such as separation and purification, filtration sterilization, and freeze-drying. It has the characteristics of high purity, high activity, tag-free, and low endotoxin. Product Properties Synonyms FGF7, FGF-7, HBGF7, HBGF-7, Heparin-binding growth factor 7, keratinocyte growth factor, KGF Expression System and Expression Range Human FGF-7 is expressed from E.coli with no tag . It contains Cys32-Thr194. Accession P21781 Molecular Weight Approximately 18.9 kDa Biological Activity Fully biologically active when compared to standard. The ED50 as determined by thymidine uptake assay using FGF-receptors transfected BaF3 cells is less than 10 ng/ml, corresponding to a specific activity of > 1.0 × 10 5 IU/mg. Appearance Sterile-filtered white lyophilized powder. Purity Greater than 96%, detected by SDS-PAGE and HPLC. Endotoxin <1.0 EU/μ Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM PB, 0.5 M NaCl, pH 8.0 Reconstitution Before opening, it is recommended to briefly centrifuge to bring the contents to the bottom. Reconstitute in sterile distilled water or an aqueous buffer solution containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. The stock solution should be divided into aliquots and stored at ≤-20°C.   Shipping and Storage Store at -25 to -15°C, with a shelf life of 1 year after receipt of goods. After reconstitution, store at 2 to 8°C for a shelf life of 30 days. After reconstitution, store at -25 to -15°C for a shelf life of 3 months. It is recommended to aliquot the protein at the first use to avoid repeated freeze-thaw cycles.   Cautions 1. This product is for research use only.2. For your safety and health, please wear a lab coat and use disposable gloves when handling.

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FGF-10, also known as Fibroblast Growth Factor-10, is a growth factor that belongs to the fibroblast growth factor family. It plays a crucial role in the development and repair of various tissues, particularly in the respiratory and limb development. Product Properties Synonyms FGF-10, Fibroblast growth factor 10, Keratinocyte growth factor 2 Uniprot No. O15520 Source E.coli-derived human FGF-10 protein, Gln38-Ser208, with C-terminal his tag Molecular Weight Approximately 20.4 kDa. Purity > 95% as determined by SDS-PAGE. Biological Activity Human FGF-10, his tag immobilized on CM5 chip can bind human FGFR2 alpha(IIIb) with an affinity constant of 9.69 x 10 -9 M as determined in a SPR assay (Biacore 8K). Endotoxin < 1 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 to ensure the concentration is greater than 100 ug/mL.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.Please operate with lab coats and disposable gloves, for your safety. 2.This product is for research use only.

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Leukemia Inhibitory Factor (LIF) is a pleiotropic cytokine produced by a variety of cell types, including T cells, bone marrow mononuclear lineage, fibroblasts, liver, heart, and melanoma. LIF promotes the long-term maintenance of embryonic stem cells by inhibiting spontaneous differentiation. Other activities include stimulating the acute-phase protein synthesis in hepatocytes, stimulating the differentiation of cholinergic neurons, and inhibiting lipogenesis in adipocytes by inhibiting lipoprotein lipase. Although human LIF is active on mouse cells and is widely used to maintain mouse ESCs to prevent spontaneous differentiation, mouse LIF is not active on human cells because it cannot bind to the human LIF receptor. This recombinant human LIF is provided in the form of a lyophilized powder, with high activity, high purity, low endotoxin, and without any additional tags. Product Properties Synonyms CDF, DIA, Differentiation-stimulating Factor, D Factor, Emfilermin, HILDA, Melanoma-derived LPL Inhibitor, MLPLI Source E.coli-derived human LIF, Ser23-Phe202. Accession P15018 Tag None Molecular Weight Approximately 19.7 kDa. AA Sequence SPLPITPVNA TCAIRHPCHN NLMNQIRSQL AQLNGSANAL FILYYTAQGE PFPNNLDKLC GPNVTDFPPF HANGTEKAKL VELYRIVVYL GTSLGNITRD QKILNPSALS LHSKLNATAD ILRGLLSNVL CRLCSKYHVG HVDVTYGPDT SGKDVFQKKK LGCQLLGKYK QIIAVLAQAF Endotoxin < 1.0 EU/μg by the LAL method. Purity ＞ 98%, as determined by SDS-PAGE and HPLC analysis. Biological Activity The ED50 as determined by the dose-dependent proliferation of human TF-1 cells is less than 0.1 ng/mL, corresponding to a specific activity of > 1.0 × 10 ^7  IU/mg. Fully biologically active when compared to standard. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4. Physical Appearance White lyophilized powder   Shipping and Storage Store at -25 to -15°C, with a shelf life of 1 year from the date of receipt of goods.After reconstitution, store at 2 to 8°C, with a shelf life of 7 days.After reconstitution, store at -85 to -65°C, with a shelf life of 3 months.   Reconstitution Method Before opening, centrifuge briefly to bring the contents to the bottom. Reconstitute with sterile deionized water to a concentration of 0.1-1.0 mg/mL, which can be further diluted according to subsequent experimental needs; for long-term storage, it is recommended to include a carrier protein (0.1% BSA) in the dilution buffer; aliquot for a single experimental use and store at -80°C to avoid repeated freeze-thaw cycles. Cautions 1. For your safety and health, please wear a lab coat and use disposable gloves when handling.2. This product is for research purposes only.

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Members of Lipocalin family share a highly conserved fold with an eight-stranded antiparallel beta barrel, and act as a transporters, carrying small molecules to specific cells. Lipocalin-2, also known as Neutrophil Gelatinase-Associated Lipocalin (NGAL), was originally identified as a component of neutrophil granules. It is a 25 kDa protein existing in monomeric and homo- and heterodimeric forms, the latter as a dimer with human neutrophil gelatinases (MMP-9). Its expression has been observed in most tissues normally exposed to microorganism, and its synthesis is induced in epithelial cells during inflammation. Lipocalin-2 has been implicated in a variety of processes including cell differentiation, tumorigenesis, and apoptosis. Studies indicate that Lipocalin-2 binds a bacterial catecholate sidropore bound to ferric ion such as enterobactin with a subnanomolar dissociation constant (Kd = 0.41 nM). The bound ferric enterobactin complex breaks down slowly in a month into dihydroxybenzoyl serine and dihydroxybenzoic acid (DHBA). It also binds to a ferric DHBA complex with much less Kd values. Secretion of Lipocalin- 2 in immune cells increases by stimulation of Toll-like receptor as an acute phase response to infection. As a result, it acts as a potent bacteriostatic reagent by sequestering iron. Moreover, Lipocalin-2 can alter the invasive and metastatic behavior of Ras-transformed breast cancer cells in vitro and in vivo by reversing epithelial to mesenchymal transition inducing activity of Ras, through restoration of E-cadherin expression, via effects on the Ras-MAPK signaling pathway. Product Properties Synonyms NGAL, p25 Accession P80188 GeneID 3934 Source E.coli-derived Human LCN2, Gln21-Gly198. Molecular Weight Approximately 41.0 kDa. AA Sequence QDSTSDLIPA PPLSKVPLQQ NFQDNQFQGK WYVVGLAGNA ILREDKDPQK MYATIYELKE DKSYNVTSVL FRKKKCDYWI RTFVPGCQPG EFTLGNIKSY PGLTSYLVRV VSTNYNQHAM VFFKKVSQNR EYFKITLYGR TKELTSELKE NFIRFSKSLG LPENHIVFPV PIDQCIDG 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 a cell proliferation assay using human TF-1 cells is less than 0.5 ng/ml, corresponding to a specific activity of > 2.0 × 10 6 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, pH 7.4, with 0.05 % 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℃. 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 CCL16, also called Liver-expressed chemokine (LEC), Monotactin-1 (MTN-1), IL-10-inducible chemokine and so on, is expressed by the CCL16 gene located on the chromosome 17 in humans. The gene encodes a 120 a.a. residue precursor protein with a 23 a.a. residue predicted signal peptide that is cleaved to generate a 97 a.a. residue mature protein. The protein is secreted by the liver, thymus, spleen cells and showing chemotactic activity for lymphocytes and monocytes but it is distantly related to other CC chemokines, exhibiting less than 30 % sequence identity. CCL16 is highly induced by IL-10, IFN- γ and bacterial lipopolysaccharide in monmcytes and signal through CCR1, CCR2, CCR5, and CCR8. Product Properties Synonyms C-C motif chemokine 16, HCC-4, IL-10-inducible chemokine, LCC-1 Accession O15467 GeneID 6360 Source E.coli-derived human Liver-Expressed Chemokine Protein, Gln24-Gln2 Molecular Weight Approximately 11.2 kDa. AA Sequence QPKVPEWVNT PSTCCLKYYE KVLPRRLVVG YRKALNCHLP AIIFVTKRNR EVCTNPNDDW VQEYIKDPNL PLLPTRNLST VKIITAKNGQ PQLLNSQ 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 10-100 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 0.1-1.0 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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Melanoma Inhibiting Activity (MIA), also known as cartilage-derived retinoic acid-sensitive protein (CD-RAP), is an approximately 11-15 kDa protein that is secreted as a noncovalent homodimer and is structurally related to OTOR/Otoraplin and MIA-2. Mature human MIA contains a SH3 domain and shares 90% and 92% amino acid sequence identity with mouse and rat MIA, respectively. Alternative splicing generates a short isoform that lacks the SH3 domain. MIA is widely expressed in developing and regenerating cartilage and in the endothelium and parenchyma of developing lungs. MIA disrupts cellular interactions with the extracellular matrix by binding to Integrins alpha 4 beta 1 and alpha 5 beta 1. It competes with Fibronectin fragments for Integrin binding and interferes with Integrin signaling. It also functions as a chemoattractant for mesenchymal stem cells and enhances their BMP-2 and TGF-beta 3 induced differentiation into chondrocytes [tscheud]. MIA-deficient mice exhibit delayed chondrocyte differentiation but enhanced chondrocyte proliferation and cartilage repair. MIA is up-regulated in several cancers including malignant melanoma, lung adenoma, metastatic oral squamous cell carcinoma, neurofibromatosis type 1 (NF-1)-related tumors, and pancreatic cancer. It is selectively secreted and internalized from the trailing pole of migrating cells. This polarization reduces cellular attachment to the matrix at the trailing pole and contributes to directional tumor cell migration. Product Properties Synonyms CD-RAP Accession Q16674 GeneID 8190 Source E.coli-derived Human MIA, Gly25-Gln31. Molecular Weight Approximately 12.1 kDa. AA Sequence GPMPKLADRK LCADQECSHP ISMAVALQDY MAPDCRFLTI HRGQVVYVFS KLKGRGRLFW GGSVQGDYYG DLAARLGYFP SSIVREDQTL KPGKVDVKTD KWDFYCQ 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 A375 cell line is less than 5 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, 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 0.1-1.0mg/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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Mesencephalic astrocyte-derived neurotrophic factor (MANF), also known as arginine-rich, mutated in early stage tumors (ARMET) and arginine-rich protein (ARP), is a 20 kDa member of the ARMET family of proteins. The name ARMET comes from the fact that the protein was initially thought to be 50 aa longer at the N-terminus and to contain an arginine-rich region. The presence of a  specific mutation changing the previously numbered codon 50 from ATG to AGG, or deletion of that codon, has been reported in a variety of solid tumors. Human MANF is synthesized as a 179 amino acid (aa) precursor that contains a 21 aa signal sequence and a 158 aa mature chain. Mature human MANF is 99%, 98% and 96% aa identical to mature rat, mouse and  bovine  MANF,  respectively. MANF is localized to the endoplasmic reticulum (ER) and Golgi apparatus, and is also secreted. In the CNS, MANF selectively protects nigral dopaminergic neurons, versus GABAergic or serotonergic neurons, which suggests that MANF may be indicated for the treatment of Parkinson’s disease. MANF is also one of the 12 commonly unfolded protein response (UPR)-up-regulated genes. One study showed that MANF plays an important role in protecting cells against tunicamycin and thapsigargin-induced cell death. Loss of MANF renders cells more susceptible to those drugs, but also increases cell proliferation and decreases cell size. Another study showed that MANF is an endoplasmic reticulum stress response (ERSR) gene in the heart that can be induced and secreted in response to ER stresses, including ischemia, and that extracellular MANF may protect cardiac myocytes  in an autocrine and paracrine manner. Product Properties Synonyms ARMET Accession P5514 Source E.coli-derived Human MANF, Leu25-Leu182. GeneID 7873 Tag None Molecular Weight Approximately 18.2 kDa. AA Sequence LRPGDCEVCI SYLGRFYQDL KDRDVTFSPA TIENELIKFC REARGKENRL CYYIGATDDA ATKIINEVSK PLAHHIPVEK    ICEKLKKKDS QICELKYDKQ IDLSTVDLKK LRVKELKKIL DDWGETCKGC AEKSDYIRKI NELMPKYAPK AASARTDL Endotoxin < 1.0 EU/μg by the LAL method. Purity ＞ 98%, as determined by SDS-PAGE and HPLC analysis. Biological Activity The ED50 as determined by a cell proliferation assay using rat C6 cells is less than 20 μg/mL, corresponding to a specific activity of > 50 IU/mg. Fully biologically active when compared to standard. 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℃. 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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The MCP proteins are members of the CC chemokine family that signal through CCR2 and, with the exception of MCP-1, other  CCR receptors. The MCP proteins chemoattract and activate monocytes, activated Tcells, basophils, NK cells, and immature dendritic cells. The MCP family cross-reacts across species. Recombinant Human MCP-3 is a 9.0 kDa protein containing 76 amino acid residues including the four highly conserved cysteine residues present in the CC chemokines. Product Properties Synonyms NC28, Small-inducible cytokine A7 Accession P80098 Source E.coli-derived Human CCL7 protein,Gln24-Leu99. GeneID 6354 Tag None Molecular Weight Approximately 9.0 kDa. AA Sequence QPVGINTSTT CCYRFINKKI PKQRLESYRR TTSSHCPREA VIFKTKLDKE ICADPTQKWV QDFMKHLDKK TQTPKL Endotoxin < 1 EU/μg of protein as determined by LAL method Purity ＞ 97%, as determined by SDS-PAGE and HPLC analysis. Biological Activity Fully biologically active when compared to standard. The biologically active determined by a chemotaxis bioassay using human monocytes is in a concentration range of 10-100 ng/mL. 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.   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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MIC-B (MHC class I chain-related gene B) is a single-pass type I member protein. A closely related protein, MICA, shares 85% amino acid identity with MICB. It is widely expressed in many, but not all, epithelial tumors of lung, breast, kidney, ovary, prostate and colon. In addition to this, it is produced by hepatocellular carcinomas, which is only in tumor cells but not in surrounding non-cancerous tissue and can be induced by bacterial and viral infections. MICA/B are ligands for NKG2D, an activating receptor expressed on NK cells, NKT cells, gamma δ T cells, and CD8+ alpha beta T cells. Recognition of MICA/B by NKG2D results in the activation of cytolytic activity and/or cytokine production by these effector cells. MICA/B recognition is involved in tumor surveillance, viral infections, and autoimmune diseases. The release of soluble forms of MICA/B from tumors down-regulates NKG2D surface expression on effector cells resulting in the impairment of anti-tumor immune response. Product Properties Synonyms MHC class I chain-related protein B, MICB, stress inducible class I homolog Accession NP_005922 Source E.coli-derived human MIC-B protein, Ala23-Asp309. GeneID 4277 Tag None Molecular Weight Approximately 32.8 kDa. AA Sequence AEPHSLRYNL MVLSQDESVQ SGFLAEGHLD GQPFLRYDRQ KRRAKPQGQW AEDVLGAKTW DTETEDLTEN GQDLRRTLTH IKDQKGGLHS LQEIRVCEIH EDSSTRGSRH FYYDGELFLS QNLETQESTV PQSSRAQTLA MNVTNFWKED AMKTKTHYRA MQADCLQKLQ RYLKSGVAIR RTVPPMVNVT CSEVSEGNIT VTCRASSFYP RNITLTWRQD GVSLSHNTQQ WGDVLPDGNG TYQTWVATRI RQGEEQRFTC YMEHSGNHGT HPVPSGKVLV LQSQRTD Endotoxin < 1 EU/μg of protein as determined by LAL method Purity ＞ 95%, as determined by SDS-PAGE and HPLC analysis. Biological Activity The specific activity is determined by binding MICB antibody in ELISA. Fully biologically active when compared to standard. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM Tris, 150 mM NaCl, pH 8.0. 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 0.1-1.0mg/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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Midkine (MK) is a 15 kDa heparin-binding molecule originally cloned during a search for genes preferentially transcribed during retinoic acid (RA)-induced differentiation. Midkine belongs to a family of neurotrophic and developmentally-regulated heparin-binding molecules consisting of midkine, pleiotrophin (PTN/HBNF/OSF-1/HNGF-8) and the avian midkine  homolog, RI-HB (for retinoic acid-inducible heparin-binding protein). Midkine is a highly basic, nonglycosylated polypeptide that contains  five intrachain disulfide bonds. The predicted molecular weight is approximately 13.3 kDa, based on a mature peptide length of 118 amino acid residues in the mouse and 121 amino acid residues in the human. Across species, MK shows 87% identity between the human and murine proteins. Between family members, human MK is approximately 50% identical to human PTN, with conservation of all 10 cysteines. Initial structure-function studies indicate that the C-terminal half of MK contains the principal heparin-binding  site plus the molecule’s antigenicity and neurite-promoting sequences; while both the C- and N-termini are necessary for the molecule’s neurotrophic effects. Product Properties Synonyms ARAP, Midgestation and Kidney Protein, Neurite Outgrowth-promoting Factor 2, Neurite Outgrowth-promoting Protein Accession P21741 Source E.coli-derived Human Midkine, Val21-Asp143. GeneID 4192 Tag None Molecular Weight Approximately 13.4 kDa. AA Sequence VAKKKDKVKK GGPGSECAEW AWGPCTPSSK DCGVGFREGT CGAQTQRIRC RVPCNWKKEF GADCKYKFEN WGACDGGTGT KVRQGTLKKA RYNAQCQETI RVTKPCTPKT KAKAKAKKGK GKD Endotoxin < 1 EU/μg of protein as determined by LAL method Purity ＞ 97%, as determined by SDS-PAGE and HPLC analysis. Biological Activity The biological activity determined by a chemotaxis bioassay using human neutrophils is in a concentration range of 0.1-10 ng/mL. Fully biologically active when compared to standard. 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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CCL2, also called monocyte chemotactic protein- 1 (MCP- 1) or JE, is a member of the C- C or beta chemokine family that is best known as a chemotactic agent for mononuclear  cells . Human CCL2 cDNA encodes a 99 amino acid (aa) precursor protein with a   23 aa signal peptide and a 76 aa mature protein . Removal of the first 5 aa of the mature protein, including the N-terminal pyrrolidone carboxylic acid- modified glutamine, occurs naturally by metalloproteinase cleavage and down- regulates activity but not receptor binding. CCL2 may form multiple bands from 8.7- 13.5 kDa on SDS- PAGE due to non- covalent dimerization and variable carbohydrate content. Mature human CCL2 shares 78- 79% aa identity with canine, porcine and equine CCL2, while mouse and rat express a form of CCL2 that is extended by 49 aa and shares only 56% aa identity within the common region. Human CCL2 can, however, induce a response in murine cells. Product Properties Synonyms HC11, Monocyte chemoattractant protein 1, MCAF, MCP-1, Monocyte secretory protein JE, Small-inducible cytokine A2 Accession P13500 Source E.coli-derived Human CCL2 ,Gln23-Thr99. GeneID 6347 Tag None Molecular Weight Approximately 8.7 kDa. AA Sequence QPDAINAPVT CCYNFTNRKI SVQRLASYRR ITSSKCPKEA VIFKTIVAKE ICADPKQKWV QDSMDHLDKQ TQTPKT Endotoxin < 1 EU/μg of protein as determined by LAL method Purity ＞ 96%, as determined by SDS-PAGE and HPLC analysis. 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 10-100 ng/mL. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM 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 0.1-1.0mg/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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LAG-1 is CC chemokine that signals through the CCR5 receptor. LAG-1 is identical to MIP-1β (ACT II isotype) except for two amino acid substitutions; arginine for histidine at position 22 and serine for glycine at position 47 of the mature protein. LAG-1 chemoattracts monocytes, and exhibits activity as an HIV-suppressive factor. Product Properties Synonyms CCL4L1 Accession Q8NHW4 GeneID 388372 Source E.coli-derived Human CCL4L1protein,Ala24-Asn92. Molecular Weight Approximately 7.8 kDa. AA Sequence APMGSDPPTA CCFSYTARKL PRNFVVDYYE TSSLCSQPAV VFQTKRGKQV CADPSESWVQ EYVYDLELN 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 human CCR5 transfected murine BaF3 cells is less than 2.0 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 PSB. 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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Human lymphotactin (Lptn)/XCL1 (also named human SCM-1 alpha and ATAC) and its mouse homologue belong to the C or gamma subfamily of chemokines. The C chemokines lack two (the 1st and 3rd ) of the four invariant cysteine residues normally found in the CC and CXC chemokines and have an extended carboxy terminus. Human lymphotactin encodes a 114 amino acid residue precursor protein with a 21 amino acid residue predicted signal peptide. The expression of lymphotactin is abundant in some activated T cells such as activated CD8+ T cells and other class I MHC restricted T cells. Lptn expression is absent in CD4+ T cells. Human and mouse Lptn share approximately 60% amino acid sequence homology. The gene for lymphotactin has been mapped to chromosome 1 in both human and mouse. Recombinant human lymphotactin has been shown to have chemotactic activity for lymphocytes and NK cells. The orphan receptor GPR5 has been reported to be the specific receptor for Lptn. Product Properties Synonyms ATAC, C motif chemokine 1, Cytokine SCM-1, Lymphotaxin, SCM-1-alpha, Small-inducible cytokine C1, XC chemokine ligand 1 Accession P47992 GeneID 6375 Source E.coli-derived Human Lymphotactin/XCL1, Gly23-Gly114. Molecular Weight Approximately 10.2 kDa. AA Sequence GSEVSDKRTC VSLTTQRLPV SRIKTYTITE GSLRAVIFIT KRGLKVCADP QATWVRDVVR SMDRKSNTRN NMIQTKPTGT QQSTNTAVTL TG Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 98 % by SDS-PAGE and HPLC analyses. Biological Activity The biological activity determined by a chemotaxis bioassay using human T-lymphocytes is in a concentration of 10-100 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 0.1-1.0 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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CCL23 is a member of CC chemokine family and is encoded by CCL23 gene located on Chr.17 in humans, where near several other CC chemokines. Highly expressed in adult lung, liver, skeletal muscle and pancreas, this protein shows strong chemotactic activity for monocytes, resting T-lymphocytes, and neutrophils, but not for activated lymphocytes. It elicits the effects by binding to CCR1. CCL23 is reported that it can be cleaved into four forms: CCL23 (19-99), CCL23 (22-99), CCL23 (27-99), CCL23 (30-99). Product Properties Synonyms CK-BETA-8; Ckb-8; Ckb-8-1; hmrp-2a; MIP-3; MIP3 ; MPIF-1; MPIF1; SCYA23 Accession P55773 GeneID 6368 Source E.coli-derived Human Macrophage Inflammatory Protein-3, Arg22-Asn120 Molecular Weight Approximately 11.4 kDa. AA Sequence RVTKDAETEF MMSKLPLENP VLLDRFHATS ADCCISYTPR SIPCSLLESY FETNSECSKP GVIFLTKKGR RFCANPSDKQ VQVCMRMLKL DTRIKTRKN 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 T-lymphocytes is in a concentration of 10-50 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 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 0.1-1.0 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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Human CCL15 is belonging to the CC chemokine family and shares 35 % amino acid homology with human HCC1 (CCL14). CCL15 is most abundant in heart, skeletal muscle and adrenal gland, and low expressed in liver, small intestine, colon, and in certain leukocytes and macrophages of the lung. It is chemotactic for neutrophils, monocytes, and lymphocytes and elicits its effects by binding to cell surface chemokine receptors like CCR1 and CCR3. CCL15 has several cleaved chains. All of them are more potent chemoattractants than CCL15. Product Properties Synonyms HCC-2;HMRP-2B; LKN-1; LKN1; MIP-1 delta; MIP-1D; MIP-5; MRP-2Bn; NCC-3; NCC3; Accession Q16663 GeneID 6359 Source E.coli-derived Human Macrophage Inflammatory Protein-5, Ser46-Ile113 Molecular Weight Approximately 7.4 kDa. AA Sequence SFHFAADCCT SYISQSIPCS LMKSYFETSS ECSKPGVIFL TKKGRQVCAK PSGPGVQDCM  KKLKPYSI 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 T-lymphocytes is in a concentration 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 1×PBS, pH 7.2. 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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Melanoma Inhibitor Activity Protein 2 (MIA-2) encoded by MIA2 gene in humans, is a secreted cytokine that is highly expressed in liver and weakly in testis. The patients with severe fibrosis or inflammation and chronic hepatitis have higher level of MIA2 than other. Levels of MIA2 may severe as a clinically utility marker for diagnosis of hepatic disease activity and severity. The MIA2 is a member of the MIA/OTOR family, which also includes MIA, OTOR, and TANGO, and they share a Src homology-3 (SH3)-like domain. Product Properties Synonyms Melanoma inhibitory activity protein 2, MIA2 Accession Q96PC5 GeneID 117153 Source E.coli-derived HumanMIA-2 protein, Leu20-Leu119. Molecular Weight Approximately 11.4 kDa. AA Sequence LESTKLLADL KKCGDLECEA LINRVSAMRD YRGPDCRYLN FTKGEEISVY VKLAGEREDL WAGSKGKEFG YFPRDAVQIE EVFISEEIQM STKESDFLCL Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97 % by SDS-PAGE and HPLC analyses. Biological Activity Testing in progress. 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.   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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Migration Inhibitory Factor (MIF) is a secreted protein without a cleavable signal sequence and is secreted via a specialized, non-classical pathway. It is secreted by macrophages upon stimulation by bacterial lipopolysaccharide (LPS), or by M.tuberculosis antigens. MIF consists of two α-helices and six β-strands, four of which form a β-sheet. The two remaining β-strands interact with other MIF molecules, creating a trimer. Structure-function studies suggest MIF is bifunctional with segregated topology. The N- and C-termini mediate enzyme activity (in theory). Phenylpyruvate tautomerase activity (enol-to-keto) has been demonstrated and is dependent upon Pro at position 1. Amino acids 50-65(a.a.) have also been suggested to contain thiol-protein oxidoreductase activity. MIF has proinflammatory cytokine activity centered around (a.a.) 49 - 65. On fibroblasts, MIF induces, IL-1, IL-8 and MMP expression; on macrophages, MIF stimulates NO production and TNF-α release folllowing IFN-γ activation. MIF apparently acts through CD74 and CD44, likely in some form of trimeric interaction. Human MIF is active on mouse cells. Human MIF is 90 %, 94 %, 95 %, and 90 % aa identical to mouse, bovine, porcine and rat MIF, respectively. Product Properties Synonyms GIF Protein, Human; GLIF Protein, Human; MMIF Protein, Human Accession P14174 GeneID 4282 Source E.coli-derived Human Macrophage Migration Inhibitory Factor protein, Met-Ala115 Molecular Weight Approximately 12.5 kDa. AA Sequence MPMFIVNTNVPRASVPDGFLSELTQQLAQATGKPPQYIAVHVVPDQLMAFGGSSEPCALCSLHSI GKIGGAQNRSYSKLLCGLLAERLRISPDRVYINYYDMNAANVGWNNSTFA 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 specific activity is determined by binding rhCD74 in a functional ELISA. 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.   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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As the first member of membrane type (MT) MMPs, MMP-14, also known as MT1-MMP, plays an important role in extracellular matrix (ECM) remodeling by being able to degrade type I collagen, activate pro-MMP-2 and process cell adhesion molecules such as CD44 and integrin alpha V. MMP-14 is therefore a key enzyme in many physiological and pathological processes such as angiogenesis and tumor invasion. Structurally, MMP-14 consists of the following domains: a pro domain containing the furin cleavage site, a catalytic domain containing the zinc-binding site, a hinge region, a hemopexin-like domain, a transmembrane domain, and a cytoplamasic tail. Product Properties Synonyms MMP-X1, MT-MMP 1, MT1-MMP Accession P50281 GeneID 4323 Source E.coli-derived Human MMP-14 protein, Ala21-Gly284. Molecular Weight Approximately 29.6 kDa. AA Sequence ALASLGSAQS SSFSPEAWLQ QYGYLPPGDL RTHTQRSPQS LSAAIAAMQK FYGLQVTGKA DADTMKAMRR PRCGVPDKFG AEIKANVRRK RYAIQGLKWQ HNEITFCIQN YTPKVGEYAT YEAIRKAFRV WESATPLRFR EVPYAYIREG HEKQADIMIF FAEGFHGDST PFDGEGGFLA HAYFPGPNIG GDTHFDSAEP WTVRNEDLNG NDIFLVAVHE LGHALGLEHS SDPSAIMAPF YQWMDTENFV LPDDDRRGIQ QLYG Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95 % by SDS-PAGE and HPLC analyses. Biological Activity Test in Process. 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 Tris-HCl, pH 7.4, 300 mM NaCl, 3 mM CaCl2, 10 μM ZnCl2, with 30% glycerol. 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 -15℃ to -25℃ 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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Macrophage colony stimulating factor 1, also known as CSF-1 and M-CSF, is a one-way membrane protein that forms homodimers or heterodimers via disulfide bonds. M-CSF is a major regulator of macrophage survival, proliferation and differentiation. M-CSF can promote monocyte survival, monocyte transformation to macrophage and macrophage proliferation. Product Properties Synonyms CSF-1,Lanimostim Source Recombinant Human M-CSF Protein is expressed from HEK293 Cells with His tag at the C-terminal. It contains Glu33-Arg255. Molecular Weight Approximately 27.08 kDa. Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95 % by SDS-PAGE and HPLC analyses. Endotoxin < 0.01 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.22 μm filtered concentrated 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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CCL22 is a protein that in humans is encoded by the CCL22 gene, which locates on the Chr. 16. The protein is highly expressed in macrophage, monocyte-derived dendritic cell and thymus, additionally, also detected in the tissues of thymus, lymph node and appendix. CCL22 can bind to CCR4, and is a chemoattractant for monocytes, monocyte-derived dendritic cells, and natural killer cells, but not for neutrophils, eosinophils, and resting T-lymphocytes. After secreted from monocyte-derived dendritic cells, the protein can be proteolytic cleaved into three forms: MDC (3-69), MDC (5-69), MDC (7-69). Product Properties Synonyms A-152E5.1n ABCD-1; DC/B-CK; MDC ; SCYA22 ; STCP-1 Accession O00626 GeneID 6367 Source E.coli-derived human Macrophage-Derived Chemokine Protein, Gly25-Gln93 Molecular Weight Approximately 8.1 kDa. AA Sequence GPYGANMEDS VCCRDYVRYR LPLRVVKHFY WTSDSCPRPG VVLLTFRDKE ICADPRVPWV KMILNKLSQ Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97 % by SDS-PAGE and HPLC analyses. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.22 μm filtered concentrated solution in 20 mM PB, pH7.4, 500 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.   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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The MCP proteins are members of the CC chemokine family that signal through CCR2 and, with the exception of MCP-1, other CCR receptors. The MCP proteins chemoattract and activate monocytes, activated Tcells, basophils, NK cells, and immature dendritic cells. The MCP family cross-reacts across species. Recombinant Human MCP-3 is a 9.0 kDa protein containing 76 amino acid residues including the four highly conserved cysteine residues present in the CC chemokines.   Product Properties   Synonyms Interleukin-6,BSF2,HSF,IFNB2 Accession P80098 GeneID 6354 Source E.coli-derived Human CCL7 protein,Gln24-Leu99. Molecular Weight Approximately 9.0 kDa AA Sequence QPVGINTSTT CCYRFINKKI PKQRLESYRR TTSSHCPREA VIFKTKLDKE ICADPTQKWV QDFMKHLDKK TQTPKL 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 determined by a chemotaxis bioassay using human monocytes is in a concentration range of 10-100 ng/mL. Endotoxin < 1 EU/μg of 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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Human CCL13 is belonging to the CC chemokine family and is encoded by the gene CCL13. CCL13 (MCP-4) shares 56-61 % sequence identity with MCP-1 (CCL2) and MCP-3 (CCL7) and is 60 % identical to Eotaxin (CCL11). CCL13 was a potent chemoattractant for monocytes and eosinophils and stimulated histamine release from basophils. CCL13 can induce a calcium flux in HEK-293 cells transfected with the receptor CCR2B and CCR3. That shows the function receptors of CCL3 are CCR2B and CCR3.   Product Properties   Synonyms CCL13 Protein, Human; CKb10 Protein, Human; MCP-4 Protein, Human; MCP4 Protein, Human; NCC-1 Protein, Human; NCC1 Protein, Human; SCYA13 Protein, Human; SCYL1 Protein, Huma Accession Q99616 GeneID 6357 Source E.coli-derived human Monocyte Chemotactic Protein-4, Gln24-Thr98 Molecular Weight Approximately 8.6 kDa. AA Sequence QPDALNVPST CCFTFSSKKI SLQRLKSYVI TTSRCPQKAV IFRTKLGKEI CADPKEKWVQ NYMKHLGRKA HTLKT 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 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 μm filtered concentrated solution in 20 mM PBS, 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 0.1-1.0 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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CXCL9, a member of the alpha subfamily of chemokines that lack the ELR domain, was initially identified as a lymphokine-activated gene in mouse macrophages. Human CXCL9 was subsequently cloned using mouse MIG cDNA as a probe. The human CXCL9 cDNA encodes a 125 amino acid residue precursor protein with a 22 amino acid residue signal peptide that is cleaved to yield a 103 amino acid residue mature protein.The carboxy-terminal residues of CXCL9 are prone to proteolytic cleavage resulting in size heterogeneity of natural and recombinant CXCL9.The CXCL9 gene is induced in macrophages and in primary glial cells of the central nervous system specifically in response to IFN-gamma. CXCL9 has been shown to be a chemoattractant for activated T-lymphocytes and TIL. And it elicits their chemotactic functions by interacting with the chemokine receptor CXCR3.   Product Properties   Synonyms Monokine-like Protein  Accession Q07325 GeneID 4283 Source E.coli-derived Human MIG/CXCL9, Thr23-Thr125. Molecular Weight Approximately 11.7 kDa. AA Sequence TPVVRKGRCS CISTNQGTIH LQSLKDLKQF APSPSCEKIE IIATLKNGVQ TCLNPDSADV  KELIKKWEKQ VSQKKKQKNG KKHQKKKVLK VRKSQRSRQK KTT 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 peripheral blood T-lymphocytes is in a concentration range of 10-100 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, 50 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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Myoglobin is a member of the globin superfamily and is predominantly expressed in skeletal and cardiac muscles. It forms a monomeric globular haemoprotein that is primarily responsible for the storage and facilitated transfer of oxygen from the cell membrane to the mitochondria. This protein also plays a role in regulating physiological levels of nitric oxide.   Product Properties   Accession P02144 GeneID 4151 Source E.coli-derived Human Myoglobin, Gly2-Gly154. Molecular Weight Approximately 17.1 kDa. AA Sequence GLSDGEWQLV LNVWGKVEAD IPGHGQEVLI RLFKGHPETL EKFDKFKHLK SEDEMKASED LKKHGATVLT ALGGILKKKG HHEAEIKPLA QSHATKHKIP VKYLEFISEC IIQVLQSKHP GDFGADAQGA MNKALELFRK DMASNYKELG FQG Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95% by SDS-PAGE. Biological Activity Data not available. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Supplied as a 0.2 μm filtered solution in 25 mM Tris-HCl, pH 8.0, with 50 % glycerol. 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℃ 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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NOV is a member of the CCN family of secreted, cysteine-rich regulatory proteins. The full-length NOV protein contains four structural domains that confer distinct, and sometimes opposing, biological activities. Elevated expression of NOV is associated with certain tumors, including Wilm’s tumor and most nephroblastomas. However, in other tumor types and certain cancer cell lines, increased tumorigenicity and proliferation is correlated with decreased NOV expression. Additionally, NOV induces cell adhesion and cell migration by signaling through specific cell-surface integrins, and by binding to heparin sulfate proteoglycans and to fibulin 1C. NOV has also been reported to exert proangiogenic activities.   Product Properties   Synonyms Nephroblastoma Overexpressed gene, CCN3, IGFBP9, NovH Accession P48745 GeneID 4856 Source E.coli-derived Human NOVprotein,Gln28-Met357. Molecular Weight Approximately 36.2 kDa. AA Sequence MQVAATQRCP PQCPGRCPAT PPTCAPGVRA VLDGCSCCLV CARQRGESCS DLEPCDESSG LYCDRSADPS NQTGICTAVE GDNCVFDGVI YRSGEKFQPS CKFQCTCRDG QIGCVPRCQL DVLLPEPNCP APRKVEVPGE CCEKWICGPD EEDSLGGLTL AAYRPEATLG VEVSDSSVNC IEQTTEWTAC SKSCGMGFST RVTNRNRQCE MLKQTRLCMV RPCEQEPEQP TDKKGKKCLR TKKSLKAIHL QFKNCTSLHT YKPRFCGVCS DGRCCTPHNT KTIQAEFQCS PGQIVKKPVM VIGTCTCHTN CPKNNEAFLQ ELELKTTRGK M 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 a cell proliferation assay using murine Balb/c 3T3 cells is less than 1.0 μg/mL, corresponding to a specific activity of > 1000 IU/mg. 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 Tris-HCl, pH 8.6, 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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Nesfatin-1 (NEFA Encoded Satiety and Fat-influencing protein 1) is a secreted, 10 kDa peptide derived from the translation product of the NUCB2 gene. Human Nesfatin-1 shares 85% aa identity with mouse Nesfatin-1. It is a naturally occurring protein and originally identified as a hypothalamic neuropeptide. Additionally, Nesfatin can be found in other areas of brain, and in pancreatic isletsβ-cells, gastric endocrine cells and adipocytes. It is responsible for regulating appetite and production of body fat. Excess nesfatin-1 in the brain leads to a loss of appetite, less frequent hunger, a 'sense of fullness', and a drop in body fat and weight. A lack of nesfatin-1 in the brain leads to an increase of appetite, more frequent episodes of hunger, an increase of body fat and weight, and the inability to 'feel full'.   Product Properties   Synonyms Nucleobindin 2 Accession P80303 GeneID 4925 Source E.coli-derived human Nesfatin-1 protein, Val25-Leu106. Molecular Weight Approximately 9.6 kDa. AA Sequence VPIDIDKTKV QNIHPVESAK IEPPDTGLYY DEYLKQVIDV LETDKHFREK LQKADIEEIK SGRLSKELDL VSHHVRTKLD EL Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >95% by SDS-PAGE and HPLC analyses. Biological Activity The biological activity is tested by in vivo assay using healthy wild type male mice (C57BL/6J). 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 0.1-1.0 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℃ 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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The neuregulin family of structurally related glycoproteins comprises products from four distinct but related genes, Nrg-1, Nrg-2, Nrg-3, and Nrg-4. All NRG1 isoforms contain an EGF-like domain that is required for their direct binding to the ErbB3 or ErbB4 receptor tyrosine kinases. The ErbB3 or ErbB4 subsequently recruits and heterodimerizes with ErbB2, resulting in tyrosine phosphorylation and NRG1 signaling.   Product Properties   Synonyms ARIA; GGF2; HGL; HRG; HRG1; MST131 Accession Q02297 GeneID 3084 Source E.coli-derived Human NRG1-α, Ser177-Lys241. Molecular Weight Approximately 7.4 kDa. AA Sequence SHLVKCAEKE KTFCVNGGEC FMVKDLSNPS RYLCKCQPGF TGARCTENVP MKVQNQEKAE ELYQK 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 serum free human MCF-7 cells is less than 40 ng/mL, corresponding to a specific activity of ＞ 2.5 × 10 4 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 solution in 20 mM PB, pH 6.0, 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℃. 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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The neuregulin family of structurally related glycoproteins comprises products from four distinct but related genes, Nrg-1, Nrg-2, Nrg-3, and Nrg-4. Through alternative splicing or the use of alternative promoters, Nrg-1 has been shown to encode more than 14 soluble or transmembrane proteins. The extracellular domain of the transmembrane NRG1 isoforms can be proteolytically cleaved to release soluble growth factors. All NRG1 isoforms contain an EGF-like domain ( alpha - or beta -splice variant that differ in their C-terminal region) that is required for their direct binding to the ErbB3 or ErbB4 receptor tyrosine kinases. The ErbB3 or ErbB4 subsequently recruits and heterodimerizes with ErbB2, resulting in tyrosine phosphorylation and NRG1 signaling. NRG1 isoforms can be classified into three major subtypes. Type I (Neu Differentiation Factor, NDF; Heregulin, HRG; Acetylcholine Receptor Inducing Activity, ARIA) and type II (Glial Growth Factor, GGF) NRG1s have an immunoglobulin (Ig)-like domain N-terminal to the EGF-like domain. Type I NRG1s differ from type II NRG1s by having a glycosylation-rich domain between the Ig-like and the EGF-like domains. Type III NRG1s (Sensory and Motor neuron-Derived Factor) lacks the Ig-like domain but has a cysteine rich domain (CRD) instead. NRG1 isoforms show distinct spatial and temporal expression patterns. These proteins play important roles during development of both the nervous system and the heart. They have been shown to regulate the selective expression of neurotransmitter receptors in neurons and at the neuromuscular junction, and promote the differentiation and development of Schwann cells from neural crest stem cells. NRG1s have also been shown to be involved in the establishment of the oligodendroglial lineage.   Product Properties   Synonyms ARIA; GGF; GGF2; HGL; HRG; Neuregulin-1 beta 1; NRG1 beta 1 Accession Q02297 GeneID 3084 Source E.coli-derived Human NRG1-β1, Ser177-Glu241. Molecular Weight Approximately 7.5 kDa. AA Sequence SHLVKCAEKE KTFCVNGGEC FMVKDLSNPS RYLCKCPNEF TGDRCQNYVM ASFYKHLGIE FMEAE 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 serum free human MCF-7 cells is less than 0.5 ng/mL, corresponding to a specific activity of > 2.0 × 10 6 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 solution in 1 × 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℃. 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 to -70 °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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Neuregulin 1 or NRG1 is one of four proteins in the neuregulin family that act on the EGFR family of receptors. Nrg-1 has been shown to encode more than 14 soluble or transmembrane proteins. The extracellular domain of the transmembrane NRG1 isoforms can be proteolytically cleaved to release soluble growth factors. All NRG1 isoforms contain an EGF-like domain ( alpha - or beta -splice variant that differ in their C-terminal region) that is required for their direct binding to the ErbB3 or ErbB4 receptor tyrosine kinases. NRG1 is a trophic factor that has been implicated in neural development, neurotransmission, and synaptic plasticity. Neuregulin 1 (NRG1) is essential for the development and function of multiple organ systems, and its dysregulation has been linked to diseases such as cancer and schizophrenia. NRG1 is a schizophrenia candidate gene and plays an important role in brain development and neural function.   Product Properties   Synonyms Heregulin-beta1, HRG1 Accession Q02297 GeneID 3084 Source E.coli-derived Human NRG1-β2, Ser177-Gln237. Molecular Weight Approximately 7.0 kDa. AA Sequence SHLVKCAEKE KTFCVNGGEC FMVKDLSNPS RYLCKCPNEF TGDRCQNYVM ASFYKAEELY Q 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 serum free human MCF-7 cells is less than 5 ng/mL, corresponding to a specific activity of > 2.0 × 10 5 U/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 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℃. 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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Neuritin also known as NRN1 and CPG15 is a neurotrophic factor, which is expressed in response to induction of neuronal activity by NGF, BDNF, NT3 and other neural stimulators. It promotes neurite outgrowth and especially branching of neuritic processes in primary hippocampal and cortical cells. Recombinant Human Neuritin is a covalently disulfide-linked homodimer, consisting of two 9.7 kDa polypeptide monomers, each containing 88 amino acid residues. It shares 99 % and 97 % a.a. sequence identity with murine and rat neuritin, respectively.   Product Properties   Synonyms NRN1 Accession Q9NPD7 GeneID 51299 Source E.coli-derived Human Neuritin, Ala28-Asn115. Molecular Weight Approximately 19.4 kDa. AA Sequence AGKCDAVFKG FSDCLLKLGD SMANYPQGLD DKTNIKTVCT YWEDFHSCTV TALTDCQEGA KDMWDKLRKE SKNLNIQGSL FELCGSGN 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 by a cell proliferation assay using rat C6 cells is less than 25 ng/mL, corresponding to a specific activity of > 4.0 × 10^4 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 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℃. 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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Neuron specific enolase (NSE), also known as ENO2 or gamma-enolase, is a dimeric, Mg 2+ -dependent enzyme that catalyzes the dehydration of 2-phospho-D glycate (PGA) to phosphoenolpyruvate (PEP) in the glycolytic pathway and catalyzes the reverse reaction in gluconeogenesis. NSE is a 47.1 kDa member of the Enolase family of enzymes. It is expressed in developing neurons and glia, is known to catalyze the generation of phosphoenolpyruvate, and is suggested to possess neurotrophic activity for neurons, likely through an extracellular mechanism. Human Neuron-specific Enolase is 433 amino acids (aa) in length. The enzymatic site spans most of the length of the molecule. Neuron-specific Enolase exists as both a noncovalently-linked homodimer, or heterodimer with alpha-enolase. Full-length human Enolase 2 shares 99% aa identity with both murine and canine Enolase 2. It shares 83% aa identity with human enolases 1 and 3.   Product Properties   Synonyms 2-phospho-D-glycerate hydrolyase, ENO2, Enolase 2, gamma-Enolase, Neural enolase, neurone-specific enolase, Neuron-specific enolase, NSE Accession P09104.3 GeneID 2026 Source E.coli-derived human NSE protein, Ser2-Leu434. Molecular Weight Approximately 47.1 kDa. AA Sequence SIEKIWAREI LDSRGNPTVE VDLYTAKGLF RAAVPSGAST GIYEALELRD GDKQRYLGKG VLKAVDHINS TIAPALISSG LSVVEQEKLD NLMLELDGTE NKSKFGANAI LGVSLAVCKA GAAERELPLY RHIAQLAGNS DLILPVPAFN VINGGSHAGN KLAMQEFMIL PVGAESFRDA MRLGAEVYHT LKGVIKDKYG KDATNVGDEG GFAPNILENS EALELVKEAI DKAGYTEKIV IGMDVAASEF YRDGKYDLDF KSPTDPSRYI TGDQLGALYQ DFVRDYPVVS IEDPFDQDDW AAWSKFTANV GIQIVGDDLT VTNPKRIERA VEEKACNCLL LKVNQIGSVT EAIQACKLAQ ENGWGVMVSH RSGETEDTFI ADLVVGLCTG QIKTGAPCRS ERLAKYNQLM RIEEELGDEA RFAGHNFRNP SVL Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >96% by SDS-PAGE and HPLC analyses. Biological Activity Testing in progress. 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 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℃. 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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Neurotrophin-3 (NT-3) is a member of the NGF family of neurotrophic factors (also named neurotrophins) that are required for the differentiation and survival of specific neuronal subpopulations in both the central as well as the peripheral nervous systems. The NT-3 cDNA encodes a 257 amino acid residue precursor protein with a signal peptide and a proprotein that are cleaved to yield the 119 amino acid residue mature NT-3. The amino acid sequence of mature NT-3 is identical in human, mouse and rat. The neurotrophin family is comprised of at least four proteins including NGF, BDNF, NT-3, and NT-4/5. These secreted cytokines are synthesized as prepropeptides that are proteolytically processed to generate the mature proteins.   Product Properties   Synonyms HDNF ; NGF-2 ; NGF2 ; NT-3; NT3 Accession P20783-1 Source E. coli-derived human NT-3 protein, Tyr139-Thr257 Molecular Weight Approximately 13.8 kDa. AA Sequence YA EHKSHRGEYS VCDSESLWVT DKSSAIDIRG HQVTVLGEIK TGNSPVKQYF YETRCKEARP VKNGCRGIDD KHWNSQCKTS QTYVRALTSE NNKLVGWRWI RIDTSCVCAL SRKIGRT Tag None Purity > 90% by SDS-PAGE. concentration 0.46 mg/mL Biological Activity Measured by its binding ability in a functional ELISA. Immobilized human NT3 at 2 μg/mL (100 μL/well) can bind human TrkB-Fch. The EC50 of human TrkB-Fch is 120-350 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 5.2.   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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Neurotrophin-4 (NT-4), is a member of the NGF family of neuronal and epithelial growth factors. Neurotrophins have six conserved cysteine residues that are involved in the formation of three disulfide bonds.Mature human NT-4 shares 91% and 95% aa sequence identity with mouse and rat NT-4/5, respectively. The mature protein is secreted as a homodimer and can also form heterodimers with BDNF or NT-3. NT-4 binds and induces receptor dimerization and activation of TrkB. NT-4 promotes the development and survival of selected peripheral and CNS neurons.   Product Properties   Synonyms Neurotrophin-5, NT-5; Neurotrophin-4 ;GLC10 Accession P34130 GeneID 4909 Source E.coli-derived Human NT-4, G81-A210, with an N-terminal Met. Molecular Weight Approximately 28.1 kDa. AA Sequence MGVSETAPAS RRGELAVCDA VSGWVTDRRT AVDLRGREVE VLGEVPAAGG SPLRQYFFET RCKADNAEEG GPGAGGGGCR GVDRRHWVSE CKAKQSYVRA LTADAQGRVG WRWIRIDTAC VCTLLSRTGR A 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 the dose-dependent induction of choline acetyl transferase activity in rat basal forebrain primary septal cell cultures is less than 50 ng/mL, corresponding to a specific activity of > 2.0 × 10 4 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 5.5. 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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Neurturin is a member of the GDNF family of ligands, which include glial cell-derived neurotrophic factor (GDNF), Neurturin, Persephin, and Artemin. GDNF family proteins are distant members of the Transforming Growth Factor beta (TGF-beta ) superfamily. Similarly to other TGF-beta family proteins, Neurturin is synthesized as a precursor protein that is cleaved at the dibasic cleavage site (RXXR) to release the carboxy-terminal domain. The carboxy-terminal domain of Neurturin contains the characteristic seven conserved cysteine residues necessary for the formation of the cysteine-knot and the single interchain disulfide bond. Biologically active human Neurturin is a disulfide-linked homodimer of the carboxy-terminal 102 amino acid residues. Mature human Neurturin shares approximately 92% amino acid sequence identity with mouse Neurturin. Mature Neurturin also shares about 40% similarities with the other three members of the GDNF family ligands. Unlike other members of TGF-beta family, bioactivities of all GDNF family ligands are mediated through a unique multicomponent receptor complex composed of high affinity ligand binding component (GFR alpha -1-GFR alpha -4) and a common signaling component (cRET receptor tyrosine kinase). Each member of the GDNF family ligands has its preferred binding protein. Neurturin preferentially binds to GFR alpha -2 but can also bind GFR alpha -1 at higher concentrations. Neurturin had been shown to promote the survival of a variety of neurons including sympathetic, sensory, and central nervous system neurons. Neurturin is expressed in both neuronal and non-neuronal tissues.   Product Properties   Synonyms NRTN; NTN Accession Q99748 GeneID 4902 Source E.coli-derived Human Neurturin, Ala96-Val197. Molecular Weight Approximately 23.4 kDa. AA Sequence ARLGARPCGL RELEVRVSEL GLGYASDETV LFRYCAGACE AAARVYDLGL RRLRQRRRLR RERVRAQPCC RPTAYEDEVS FLDAHSRYHT VHELSARECA CV Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 96% by SDS-PAGE and HPLC analyses. Biological Activity The biologically active as determined by its binding ability in a functional ELISA. 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 30 mM Citrate Sodium, pH 4.2, 400 mM NaCl, 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 to a concentration of 0.5 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℃ 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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Neutrophil Activating Peptide 2 (NAP-2), also known as Chemokine (C-X-C motif) ligand 7 (CXCL7) and Pro-platelet basic protein (PPBP), is a member of the CXC chemokines. NAP-2 is found in the alpha-granules of human platelets. Nap-2 / PPBP / CXCL7 is released in large amounts from platelets following their activation. Similar to other ELR domain containing CXC chemokines such as IL-8 and the GRO proteins, NAP-2 has been shown to bind CXCR2 and to chemoattract and activate neutrophils. Nap-2 / PPBP / CXCL7 has been shown to stimulate various cellular processes including DNA synthesis, mitosis, glycolysis, intracellular cAMP accumulation, prostaglandin E2 secretion, and synthesis of hyaluronic acid and sulfated glycosaminoglycan. It also stimulates the formation and secretion of plasminogen activator by synovial cells. Nap-2 is a ligand for CXCR1 and CXCR2, and Nap-2, Nap-2 (73), Nap-2 (74), Nap-2 (1-66), and most potent Nap-2 (1-63).   Product Properties   Synonyms CXCL7, LDGF, MDGF, Small-inducible cytokine B7 Accession P02775 GeneID 5473 Source E.coli-derived Human NAP-2/CXCL7, Ala59-Asp128. Molecular Weight Approximately 7.6 kDa. AA Sequence AELRCMCIKT TSGIHPKNIQ SLEVIGKGTH CNQVEVIATL KDGRKICLDP DAPRIKKIVQ KKLAGDESAD 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 peripheral blood neutrophils is in a concentration range of 1.0-10.0 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, 50 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℃. 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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Noggin is a bone morphogenetic protein (BMP) antagonist expressed in Spemann's organizer. It inhibits TGF-β family ligands and preventing them from binding to their corresponding receptors.   Product Properties   Synonyms NOG, SYM1, symphalangism 1 (proximal), synostoses (multiple) syndrome 1, SYNS1 Uniprot No. Q13253 Source HEK293 cells -derived human Noggin protein, Gln28-Cys232, with a His tag at the C-terminal Molecular Weight The protein migrates as 30 KDa under reducing (R) condition (SDS-PAGE) . Activity Measured by its ability to bind BMP2 with Elisa method . Optimal concentrations should be determined by each laboratory for each application Purity > 95% as determined by SDS-PAGE. Endotoxin <1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered solution in PBS. Reconstitution It is recommended that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute the lyophilized powder in ddH2O or PBS up to 100 μg/ml.   Storage   The product should be stored at -85~-65℃ for 1 year from date of receipt.   Caution   1.Please operate with lab coats and disposable gloves,for your safety. 2.This product is for research use only.

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Cardiotrophin-like cytokine (CLC), also referred to as novel neurotrophin-1 (NNT-1) or B cell-stimulating factor-3 (BSF-3), is a new member of the IL-6 family of structurally related cytokines that includes IL-6, CNTF, LIF, CT-1, IL-11 and OSM. All family members share the receptor subunit gp130 that belong to the type I cytokine receptor superfamily. Ligand binding leads to gp130 homodimerization or heterodimerization (with LIF receptor or OSM receptor beta ), and induces cell signaling and functional activity. For several family members, including CNTF, IL-6, and IL-11, binding of the ligand to a specific receptor alpha subunit (CNTF R alpha, IL-6 R alpha, or IL-11 R alpha ) is required prior to gp130 homo- or hetero-dimerization. CLC cDNA encodes a 225 amino acid (aa) residue precursor protein with a putative 27 aa residue signal peptide that is cleaved to yield the mature protein. Among the IL-6 family, CLC is the most homologous to cardiotrophin, having 29% aa sequence homology. CLC has been shown to bind with the soluble orphan receptor cytokine-like factor-1 (CLF) to form a heterodimeric composite cytokine that subsequently interacts with the membrane- associated CNTF R alpha to initiate gp130-LIF R dimerization and cell signaling. Alternatively, when co-expressed within the cell, CLC can complex with soluble CNTF R alpha to form an alternate composite cytokine that is secreted. This composite cytokine is also capable of initiating gp130-LIF R dimerization. The E. coli-expressed CLC can initiate cell signaling via the tripartite membrane- associated CNTF R alpha and gp130-LIF R. E. coli-expressed CLC does not bind efficiently with soluble CNTF R alpha in solution to initiate cell signaling on cells expressing gp130 and LIF R.   Product Properties   Synonyms Cardiotrophin-like cytokine factor 1, BSF-3 Accession Q9UBD9 GeneID 23529 Source E.coli-derived Human NNT-1/BCSF-3, Leu28-Phe225. Molecular Weight Approximately 22.3 kDa. AA Sequence LNRTGDPGPG PSIQKTYDLT RYLEHQLRSL AGTYLNYLGP PFNEPDFNPP RLGAETLPRA TVDLEVWRSL NDKLRLTQNY EAYSHLLCYL RGLNRQAATA ELRRSLAHFC TSLQGLLGSI AGVMAALGYP LPQPLPGTEP TWTPGPAHSD FLQKMDDFWL LKELQTWLWR SAKDFNRLKK KMQPPAAAVT LHLGAHGF 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 TF-1 cells is less than 4 ng/mL, corresponding to a specific activity of > 2.5 × 10 5 IU/mg in the presence of human CNTF R alpha. 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 30% Acetonitrile and 0.1% 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℃. 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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Brain-type Natriuretic Peptide (BNP) is a nonglycosylated peptide that is produced predominantly by ventricular myocytes and belongs to the natriuretic peptide family. Proteolytic cleavage of the 12 kDa BNP precursor gives rise to N-terminal Pro‑BNP (NT-proBNP) and mature BNP. Plasma NT-proBNP is a marker for congestive heart failure, while mature BNP (aa 103‑134) promotes vasodilation and fluid and sodium excretion. Human BNP precursor shares 29% and 51% aa sequence identity with mouse and porcine BNP precursor, respectively.   Product Properties   Synonyms Natriuretic peptides B, Gamma-brain natriuretic peptide Accession P16860 GeneID 4879 Source E.coli-derived Human NT-pro-BNP, His27-Arg102. Molecular Weight Approximately 8.5 kDa. AA Sequence HPLGSPGSAS DLETSGLQEQ RNHLQGKLSE LQVEQTSLEP LQESPRPTGV WKSREVATEG IRGHRKMVLY TLRAPR Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 98 % by SDS-PAGE and HPLC analyses. Biological Activity Data is not available. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20mM Tris-HCl, pH 8.0, 150mM 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℃. 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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Oncostatin M (OSM) is a growth and differentiation factor that participates in the regulation of neurogenesis, osteogenesis and hematopoiesis. It stimulates the proliferation of fibroblasts, smooth muscle cells and Kaposi’s sarcoma cells, but inhibits the growth of some normal and tumor cell lines.   Product Properties   Synonyms Oncostatin M/oncostatin-M; Uniprot No. P13725 Source Human OSM Protein is expressed from HEK293 without tag. It contains Ala26-Arg221. Molecular Weight The protein has a predicted 25.8 kDa Purity > 95% as determined by SDS-PAGE. Biological Activity The ED50 as determined by a cell proliferation assay using human TF-1 cells is 5-30 pg/mL. Endotoxin < 0.01 EU per 1μg of the protein by the LAL method. Formulation Dissolved in sterile PBS buffer. Concentration 0.2 mg/ml   Storage   The product should be stored at -85~-65℃ for 1 year from date of receipt. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Caution   1. Please operate with lab coats and disposable gloves,for your safety. 2. This product is for research use only.

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Osteoprotegerin (OPG), also called OCIF (osteoclastogenesis inhibitory factor) is a secreted 55-60 kDa protein that regulates bone density. As a member of the tumor necrosis factor receptor (TNFR) superfamily of proteins, it is designated TNFRSF11B. Human OPG cDNA encodes 401 amino acids (aa) including a 21 aa signal peptide and a 380 aa mature soluble protein with four TNFR domains, two death domains and a heparin-binding region. The cysteine-rich TNFR domains are essential for ligand interaction, while a cysteine at the C-terminus mediates homodimerization. Mature human OPG shares 86%, 87%, 92%, 92% and 88% amino acid sequence identity with mouse, rat, equine, canine and bovine OPG, respectively. OPG is widely expressed and constitutively released as a homodimer by mesenchymal stem cells, fibroblasts and endothelial cells. Regulation of its expression by estrogen, parathyroid hormone and cytokines is complex and changes with age. OPG has been called a decoy receptor for the TNF superfamily ligands, TRANCE (tumor necrosis factor-related activation-induced cytokine), also called RANK L (receptor activator of NF kappa B ligand), and TRAIL (TNF-related apoptosis-inducing ligand), which also bind TNF family receptors RANK and TRAIL receptors 1-4, respectively. TRAIL decreases the release of OPG from cells that express it, while OPG inhibits TRAIL-induced apoptosis. Expression of RANK L on the cell surface, and thus its ability to stimulate osteoclastogenesis, is regulated by OPG by intracellular and extracellular mechanisms. Within osteoblasts, interaction of the basic domain of OPG with RANK L in the Golgi inhibits RANK L secretion.   Product Properties   Synonyms TNFRSF11B, Osteoclastogenesis Inhibitory Factor, Tumor Necrosis Factor Receptor Superfamily Member 11B Accession O00300 GeneID 4982 Source E.coli-derived Human OPG, Glu22-Lys194. Molecular Weight Approximately 19.7 kDa. AA Sequence ETFPPKYLHY DEETSHQLLC DKCPPGTYLK QHCTAKWKTV CAPCPDHYYT DSWHTSDECL YCSPVCKELQ YVKQECNRTH NRVCECKEGR YLEIEFCLKH RSCPPGFGVV QAGTPERNTV CKRCPDGFFS NETSSKAPCR KHTNCSVFGL LLTQKGNATH DNICSGNSES TQK 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 neutralizing the stimulation of U937 cells is less than 10 ng/mL, corresponding to a specific activity of > 1.0 × 10 5 IU/mg in the presence of 10 ng/mL soluble rHuRANKL (sRANKL). 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,150 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℃ 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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Osteoprotegerin (OPG), also called OCIF (osteoclastogenesis inhibitory factor) is a secreted 55-60 kDa protein that regulates bone density. As a member of the tumor necrosis factor receptor (TNFR) superfamily of proteins, it is designated TNFRSF11B. Human OPG cDNA encodes 401 amino acids (aa) including a 21 aa signal peptide and a 380 aa mature soluble protein with four TNFR domains, two death domains and a heparin-binding region. The cysteine-rich TNFR domains are essential for ligand interaction, while a cysteine at the C-terminus mediates homodimerization. Mature human OPG shares 86%, 87%, 92%, 92% and 88% amino acid sequence identity with mouse, rat, equine, canine and bovine OPG, respectively. OPG is widely expressed and constitutively released as a homodimer by mesenchymal stem cells, fibroblasts and endothelial cells. Regulation of its expression by estrogen, parathyroid hormone and cytokines is complex and changes with age. OPG has been called a decoy receptor for the TNF superfamily ligands, TRANCE (tumor necrosis factor-related activation-induced cytokine), also called RANK L (receptor activator of NF kappa B ligand), and TRAIL (TNF-related apoptosis-inducing ligand), which also bind TNF family receptors RANK and TRAIL receptors 1-4, respectively. TRAIL decreases the release of OPG from cells that express it, while OPG inhibits TRAIL-induced apoptosis. Expression of RANK L on the cell surface, and thus its ability to stimulate osteoclastogenesis, is regulated by OPG by intracellular and extracellular mechanisms. Within osteoblasts, interaction of the basic domain of OPG with RANK L in the Golgi inhibits RANK L secretion. Extracellularly, OPG binding to RANK L results in clathrin-mediated internalization and degradation of both proteins. Binding of OPG by syndecan-1 heparin sulfates on multiple myeloma cells also results in OPG internalization and degradation, contributing to bone loss.   Product Properties   Accession O00300 GeneID 4982 Source Yeast-derived Human OPG-Fc, Glu22-Lys194. Molecular Weight Approximately 109.6 kDa. AA Sequence ETFPPKYLHY DEETSHQLLC DKCPPGTYLK QHCTAKWKTV CAPCPDHYYT DSWHTSDECL YCSPVCKELQ YVKQECNRTH NRVCECKEGR YLEIEFCLKH RSCPPGFGVV QAGTPERNTV CKRCPDGFFS NETSSKAPCR KHTNCSVFGL LLTQKGNATH DNICSGNSES TQKCGIDVTL EPKSSDKTHT CPPCPAPEFE GAPSVFLFPP KPKDTLMISR TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN KALPTPIEKT ISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GK Tag with an C-terminal Fc Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95 % by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by neutralizing the stimulation of U937 cells is less than 10 ng/mL, corresponding to a specific activity of > 1.0 × 10^5 IU/mg in the presence of 10 ng/mL soluble rHuRANKL (sRANKL). 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 6.0, 150 mM NaCl, 0.02 % Tween-80. 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℃ 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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OTOR also named Otoraplin and MIAL, is a 15 kDa disulfide bonded homodimer, which is secreted via the Golgi apparatus and is a member of the MIA/OTOR family. The OTOR shares high sequence identity with the mouse (90%), chicken (80%), and bullfrog (60%) orthologs and with the related human CDRAP/MIA protein (43%). Members of this family which also includes MIA, MIA2, and TANGO share a Src homology-3 (SH3)-like domain. OTOR is mainly expressed in the cochlea of the inner-ear and appears to be involved in early chondrogenesis of the otic capsule, which is required for normal inner ear development and auditory function. It is highly homologous to MIA/cartilage-derived retinoic acid-sensitive protein (CD-RAP), which is a cartilage-specific protein that is also expressed in malignant melanoma cells.   Product Properties   Synonyms Fibrocyte-derived Protein, Melanoma Inhibitory Activity-like Protein Accession Q9NRC9 GeneID 56914 Source E.coli-derived human OTOR protein, Vla18-Glu128. Molecular Weight Approximately 12.7 kDa. AA Sequence VHGIFMDRLA SKKLCADDEC VYTISLASAQ EDYNAPDCRF INVKKGQQIY VYSKLVKENG AGEFWAGSVY GDGQDEMGVV GYFPRNLVKE QRVYQEATKE VPTTDIDFFC E Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >97% by SDS-PAGE and HPLC analyses. Biological Activity Testing in progress. 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℃. 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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PTH (parathyroid hormone) is a critical hormone in the regulation of Ca++ homeostasis. PTH is secreted by the chief cells of the parathyroid glands as a polypeptide. PTH secretion is enhanced by low Ca++ concentrations and inhibited by FGF-23. In normal human plasma, PTH correlates negatively with active Vitamin D and positively with ionized calcium. Human and other mammalian PTH will bind and stimulate human or rat PTH1R, activating adenylate cyclase and increasing cAMP production. PTH promotes secretion of TRANCE/RANKL and periostin through PTH1R binding on osteoblasts and/or bone marrow stromal cells TRANCE/RANKL induces differentiation of osteoclasts, which in turn promote release of Ca++ from bone. PTH1R on osteocytes,  however, allows PTH to promote bone formation and IGF-1 production. In addition, PTH increases hematopoietic stem cell proliferation and mobilization and induces arterial vasodilation by regulating Ca++ influx in PTH1R-expressing arterial smooth muscle. In renal epithelium, PTH promotes conversion of Vitamin D to its active form, lowers Ca++ excretion and increases phosphate excretion.   Product Properties   Synonyms Parathormone, Parathyrin Accession P01270 GeneID 5741 Source E.coli-derived Human PTH1-84, Ser32-Gln115. Molecular Weight Approximately 9.4 kDa. AA Sequence SVSEIQLMHN LGKHLNSMER VEWLRKKLQD VHNFVALGAP LAPRDAGSQR PRKKEDNVLV ESHEKSLGEA DKADVNVLTK AKSQ 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 its ability to induce cAMP accumulation in murine MC3T3E1 cells is less than 50 ng/mL, corresponding to a specific activity of > 2.0×10 4 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 0.1-1.0 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℃ 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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PTHrP, also named parathyroid hormone-related protein, is belonging to the parathyroid hormone family. PTHrP is expressed in cancer cells (breast cancer, certain types of lung cancer including squamous cell lung carcinoma). The receptor for PTHrP is PTHR1. PTHrP plays a central role in regulating the hypercalcemia. Recombinant human PTHrP is a 9.9 kDa linear polypeptide of 86 amino acid residues and it shares 86 % a.a. identity with mouse PTHLH.   Product Properties   Synonyms Parathormone, Parathyrin Accession P12272 GeneID 5744 Source E.coli-derived human PTHrP protein, Ala37-Pro122. Molecular Weight Approximately 9.9 kDa. AA Sequence AVSEHQLLHD KGKSIQDLRR RFFLHHLIAE IHTAEIRATS EVSPNSKPSP NTKNHPVRFG SDDEGRYLTQ ETNKVETYKE QPLKTP Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >98% by SDS-PAGE and HPLC analyses. Biological Activity Testing in progress. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 10 mM PB, pH 6.0, 300 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℃. 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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Procalcitonin (PCT) belongs to a group of related proteins including calcitonin gene-related peptides I and II, amylin, adrenomodulin and calcitonin (CAPA peptide family). Mature PCT is expressed as a 116 amino acid (aa) protein which is subsequently cleaved into 3 parts: a 57 aa pro-region, a 32 aa Calcitonin peptide and a 21 aa Katacalcin peptide. PCT is a peptide precursor of the hormone calcitonin, the latter being involved with calcium homeostasis. PCT is produced by parafollicular cells (C cells) of the thyroid and by the neuroendocrine cells of the lung and the intestine. But its level is related to the severity of bacterial sepsis, it is considered to be one of the earliest and most specific markers of sepsis.   Product Properties   Synonyms CALC1, CALCA, Calcitonin 1, calcitonin gene-related peptide 1, CGRP, Katacalcin, Procalcitonin Accession P01258-1 GeneID 796 Source E.coli-derived human PCT/Procalcitonin protein, Ala26-Asn141. Molecular Weight Approximately 12.8 kDa. AA Sequence APFRSALESS PADPATLSED EARLLLAALV QDYVQMKASE LEQEQEREGS SLDSPRSKRC GNLSTCMLGT YTQDFNKFHT FPQTAIGVGA PGKKRDMSSD LERDHRPHVS MPQNAN Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >98% by SDS-PAGE and HPLC analyses. Biological Activity Testing in progress. 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 Tris-HCl, pH 8.0, 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℃. 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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Persephin is a secreted protein belonging to the glial cell line-derived neurotrophic factor (GDNF) family of the TGF-beta superfamily. It shares 38 - 46% amino acid (aa) identity with family members GDNF, neurturin and artemin. Persephin is expressed at very low levels in most tissues. The 156 aa, 10 - 12 kDa mature protein contains a signal sequence, a pro-domain and a 96 aa mature sequence with several cysteines that are conserved among family members. It circulates as an unglycosylated disulfide-linked homodimer. Mature human Persephin shares 81% and 80%, 89% and 87% amino acid sequence identity with mouse, rat, bovine and canine Persephin, respectively. Like other GDNF family members, Persephin acts through engagement of GRF alpha 4, a glycosylphosphatidylinositol (GPI)-linked GDNF receptor family (GRF) member that signals through the receptor tyrosine kinase RET. Persephin is reported to promote both the survival and growth of central dopaminergic and motor neurons, and kidney development. These effects are correlated with the expression patterns of GFR alpha 4, and RET. Functional GFR alpha 4 isoforms are found only in thyroid, adrenal medulla and portions of the central nervous system, and include GPI-linked, transmembrane and soluble forms. In vitro, Persephin promotes survival only in neurons which coexpress GPI-linked GFR alpha 4 with RET. This effect does not show a strong correlation to the recruitment of RET in lipid rafts seen with other GDNF family members.   Product Properties   Synonyms Persephin; PSP; PSPN Accession P06734 GeneID 2208 Source E.coli-derived Human Persephin, Ala61-Gly156. Molecular Weight Approximately 20.5 kDa. AA Sequence ALSGPCQLWS LTLSVAELGL GYASEEKVIF RYCAGSCPRG ARTQHGLALA RLQGQGRAHG GPCCRPTRYT DVAFLDDRHR WQRLPQLSAA ACGCGG 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 TT medullary thyroid cancer cells is less than 10 ng/mL, corresponding to a specific activity of > 1.0 × 10^5 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, 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℃. 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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