Cytokines

Fatty acid binding protein-3 (FABP3; also named Fatty acid binding protein 11, FABP11, H- or M- (heart or muscle) FABP, Mammary derived growth inhibitor, or MDGI) is a member of a large superfamily of lipid binding proteins that are expressed in a tissue specific manner. FABP3 is one of ten cytoplasmic FABPs that are 14-15 kDa in size and range from 126-140 amino acids (aa) in length. Although all are highly conserved in their tertiary structure, there is only modest aa identity between any two members. The FABP family members are subdivided based on organ or tissue type it was originally expressed or identified; liver- (L-FABP), intestine- (I-FABP), heart- (H-FABP), adipocyte- (A-FABP), epidermal- (E-FABP), ileal- (IL-FABP), brain- (B-FABP), myelin- (M-FABP) and testis-FABP (T-FABP). Human H-FABP, the product of the FABP3 gene, is a 132 aa cytosolic protein that shows a flattened beta -barrel structure generated by a series of antiparallel beta -strands and two alpha - helices. One molecule of FABP3 is capable of binding one long-chain fatty acid. It is suggested that ligands first bind to the outside of the molecule, and this binding subsequently induces a conformational change in the binding protein, resulting in "internalization" of the ligand. Human FABP3 is 86%, 89% and 89% aa identical to mouse, rat and canine FABP3, respectively. It also shows 29% and 32% aa identity to human L-FABP and I- FABP, respectively.   Product Properties Synonyms FABP11;HFABP;MDGI Accession P05413 GeneID 2170 Source E.coli-derived Human FABP3, Val2-Ala133. Molecular Weight Approximately 14.7 kDa. AA Sequence VDAFLGTWKL VDSKNFDDYM KSLGVGFATR QVASMTKPTT IIEKNGDILT LKTHSTFKNT EISFKLGVEF DETTADDRKV KSIVTLDGGK LVHLQKWDGQ ETTLVRELID GKLILTLTHG TAVCTRTYEK EA Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95% by SDS-PAGE. Biological Activity Testing in progress. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 mm filtered concentrated solution in 10mM PB,150 mM NaCl,1 mM DTT, 0.1 % tween-20, 5 % trehalose, 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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Fatty acid binding protein-2 (FABP-2; also named I- or intestinal FABP) is a member of a large superfamily of lipid binding proteins that are expressed in a tissue specific manner. FABP-2 is one of nine cytoplasmic FABPs that are 14-15 kDa in size and range from 126-134 amino acids (aa) in length. Although all are highly conserved in their tertiary structure, there is only modest aa identity between any two members. Nevertheless, based on aa sequence, the nine FABP family members have been shown to form three subgroups, with FABP- 2/I- FABP linked with liver/L-FABP and heart/H-FABP. The designation of a tissue type, such as intestinal, does not suggest the binding protein is universally expressed in all cell types that make up the organ or tissue. Human I-FABP, the product of the FABP-2 gene, is a 132 aa cytosolic protein that shows a flattened beta -barrel structure (called a beta -clam) generated by a series of antiparallel beta -strands and two alpha - helices. Preferred ligands for FABP-2 include sixteen to twenty carbon long chain fatty acids. It is suggested that ligands first bind to the outside of the molecule, and this binding subsequently induces a conformational change in the binding protein, resulting in "internalization" of the ligand. An Ala-to-Thr polymorphism at position #54 has been reported to potentially impact FABP-2 function. This polymorphism has been suggested to be associated with an increased risk of type II diabetes. To date, the evidence appears to be equivocal. This polymorphism may, however, have unusual metabolic effects depending upon the type of diet involved. Human FABP-2 is 78%, 82% and 86% aa identical to mouse, rat and canine FABP-2, respectively. It also shows 33% and 24% aa identity to human H-FABP and L- FABP, respectively. FABP-2 is proposed to transport fatty acids (FA) into cells, increase FA availability to enzymes, protect cell structures from FA attack, and target FA to transcription factors in the nuclear lumen.   Product Properties Synonyms IFABP; I-FABP Accession P12104 GeneID 2169 Source E.coli-derived Human FABP2, Ala2-Asp132. Molecular Weight Approximately 15.1 kDa. AA Sequence AFDSTWKVDR SENYDKFMEK MGVNIVKRKL AAHDNLKLTI TQEGNKFTVK ESSAFRNIEV VFELGVTFNY NLADGTELRG TWSLEGNKLI GKFKRTDNGN ELNTVREIIG DELVQTYVYE GVEAKRIFKK D Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97 % by SDS-PAGE and HPLC analyses. Biological Activity Data 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 PBS, pH 7.0 Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20℃. 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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Fatty acid binding protein-6 (FABP6), also known as ileal bile acid binding protein (I-BABP) and gastrotropin, is a 15 kDa cytoplasmic protein that belongs to the FABP family. It is expressed in ileal epithelium and multiple other tissues. Alternate transcription promoters generate two transcript variants, encoding a 128 aa and a 177 aa residue protein. Human FABP6 isoform 2 contains 128 amino acid residues and is believed to be acetylated on Ala2. It binds both fatty acids and bile acids and has roles in fatty acid transport and metabolism. The amino acid sequence of human FABP6 is 80%, 78%, and 75% aa identical to that of mouse, canine, and porcine FABP6, respectively.   Product Properties Synonyms I-BALB; I-BAP Accession P51161 GeneID 2172 Source E.coli-derived Human FABP6, Val2-Ala133 Molecular Weight Approximately 14.7 kDa AA Sequence VDAFLGTWKL VDSKNFDDYM KSLGVGFATR QVASMTKPTT IIEKNGDILT LKTHSTFKNT EISFKLGVEF DETTADDRKV KSIVTLDGGK LVHLQKWDGQ ETTLVRELID GKLILTLTHG TAVCTRTYEK EA Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder Purity > 95% by SDS-PAGE. Biological Activity Testing in progress. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 mm filtered concentrated solution in 10mM PB,150 mM NaCl,1 mM DTT, 0.1 % tween-20, 5 % trehalose, 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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Fibroblast growth factor 12 (FGF12) is a fibroblast growth factor homologous factor, a subset of the FGF superfamily. Human FGF-12 is synthesized as a 243 aa protein. In human Vascular smooth muscle cells (VSMCs), FGF12 expression was inhibited at the transcriptional level by platelet-derived growth factor-BB. FGF12 inhibited cell proliferation through the p53 pathway and upregulated the key factors involved in VSMC lineage differentiation, such as myocardin and serum response factor. In addition, FGF12 and other FGF11 subfamily members do not activate any fibroblast growth factor receptors (FGFRs), although they can bind to heparin with high affinity like other FGFs. FGF12 has structural similarity with FGF1 and FGF2, in that it lacks a classical signal sequence and con-tains a nuclear localization signal, resulting in the accu-mulation of FGF12 in the nucleus without any release from cells.   Product Properties Synonyms FGF12, FGF-12, FGF12B, FHF1, FHF-1, fibroblast growth factor 12, fibroblast growth factor 12 Accession NP_00410 GeneID 2257 Source E.coli-derived human FGF-12 protein, Met1-Thr181. Molecular Weight Approximately 20.5 kDa. AA Sequence MESKEPQLKG IVTRLFSQQG YFLQMHPDGT IDGTKDENSD YTLFNLIPVG LRVVAIQGVK ASLYVAMNGE GYLYSSDVFT PECKFKESVF ENYYVIYSST LYRQQESGRA WFLGLNKEGQ IMKGNRVKKT KPSSHFVPKP IEVCMYREQS LHEIGEKQGR SRKSSGTPTM NGGKVVNQDS T Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder Purity >98% by SDS-PAGE and HPLC analyses Biological Activity The biological activity was determined by its binding ability in a functional ELISA. Immobilized recombinant human FGF R4/Fc Chimera at 5 µg/mL (100 µL/well) can bind recombinant human FGF-12 with a linear range of 1.6-100 ng/mL. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH7.4, with 1 mM DTT. 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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Fibroblast growth factor 13 (FGF13), a member of the FGF11 subfamily, is a kind of intracrine protein similar to other family members including FGF11, FGF12, and FGF14. Unlike classical FGF, FGF13 exerts its bioactivities independent of fibroblast growth factor receptors (FGFRs). FGF13, a nonsecretory protein of the FGF family, is expressed in cerebral cortical neurons during development and is a candidate gene for syndromal and nonspecific forms of X-chromosome-linked mental retardation. The FGF-13 regulates glioma cell invasion and is important for bevacizumab-induced glioma invasion. FGF-13 plays a crucial role in neuron polarization and migration in the cerebral cortex. In mouse FGF-13 RNA was detected in developing central nervous system in cells, and was also found throughout the peripheral nervous system.   Product Properties Synonyms FGF13, FGF-13, FHF-2 Accession Q92913 GeneID 2258 Source E.coli-derived human FGF-13 protein, Met1-Thr245. Molecular Weight Approximately 27.6 kDa. AA Sequence MAAAIASSLI RQKRQARERE KSNACKCVSS PSKGKTSCDK NKLNVFSRVK LFGSKKRRRR RPEPQLKGIV TKLYSRQGYH LQLQADGTID GTKDEDSTYT LFNLIPVGLR VVAIQGVQTK LYLAMNSEGY LYTSELFTPE CKFKESVFEN YYVTYSSMIY RQQQSGRGWY LGLNKEGEIM KGNHVKKNKP AAHFLPKPLK VAMYKEPSLH DLTEFSRSGS GTPTKSRSVS GVLNGGKSMS HNEST Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity >95% by SDS-PAGE and HPLC analyses. Biological Activity Testing 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, pH 8.5, 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℃. 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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Fibroblast growth factor-16 (FGF16) is a member of FGF9 subfamily. All FGF family members are heparin-binding growth factors with a core 120 amino acid (aa) FGF domain that allows for a common tertiary structure. FGF-16 is most similar to FGF-9, sharing 73% aa sequence homology. Human FGF-16 shares 99% and 98.6% aa sequence identity with the mouse and rat FGF-16, respectively. FGF-16 binds to and activates FGF receptor 4. The expression pattern of FGF-16 and its effect on adipocyte proliferation suggest a role for this protein on the proliferation of embryonic brown adipose tissue. FGF16 belongs to the large FGF family, which plays key role in promoting mitosis and cell survival, and also involved in embryonic development, cell growth, tissue repair, morphogenesis, tumor growth, and invasion. Meanwhile, the expression of FGF-16 in the perinatal and postnatal heart and its functional significance in neonatal rat cardiac myocytes.   Product Properties Synonyms FGF16, FGF-16, fibroblast growth factor 16 Accession O43320 GeneID 8823 Source E.coli-derived human FGF-16 protein, Ala2-Arg207. Molecular Weight Approximately 23.6 kDa AA Sequence AEVGGVFASL DWDLHGFSSS LGNVPLADSP GFLNERLGQI EGKLQRGSPT DFAHLKGILR RRQLYCRTGF HLEIFPNGTV HGTRHDHSRF GILEFISLAV GLISIRGVDS GLYLGMNERG ELYGSKKLTR ECVFREQFEE NWYNTYASTL YKHSDSERQY YVALNKDGSP REGYRTKRHQ KFTHFLPRPV DPSKLPSMSR DLFHYR Tag None Physical Appearance Sterile Colorless liquid. Purity >98% by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by thymidine uptake assay using FGF-receptors transfected BaF3 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 20 mM Tris-HCl, 1 M NaCl, pH 9.0, with 0.02 % Tween-20, 10 % Glycerol.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -70℃ for 6 months. 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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Fibroblast growth factor-17( FGF17) is one of the fibroblast growth factor( FGF) family members and it makes up FGF8 subfamily along with FGF8 and FGF18. Mature human FGF- 17 shares 99% aa identity with mouse, rat, porcine and canine FGF- 17. The FGF domain of FGF- 17 shares the most aa identity with FGF- 8 (~75%) and FGF- 18 (~64%). Among different members of the FGF family, FGF17 and FGF8 share high sequence homology and have similar patterns of expression during embryogenesis. FGF- 17 is also expressed in adult bovine ovarian follicles and the human prostate, and its expression is increased by both benign hypertrophy and cancer of the prostate.   Product Properties Synonyms FGF17, FGF-17, fibroblast growth factor 17 Accession O60258 GeneID 8822 Source E.coli-derived human FGF-17 protein, Thr23-Thr216, with an N-terminal Met. Molecular Weight Approximately 22.6 kDa AA Sequence MTQGENHPSP NFNQYVRDQG AMTDQLSRRQ IREYQLYSRT SGKHVQVTGR RISATAEDGN KFAKLIVETD TFGSRVRIKG AESEKYICMN KRGKLIGKPS GKSKDCVFTE IVLENNYTAF QNARHEGWFM AFTRQGRPRQ ASRSRQNQRE AHFIKRLYQG QLPFPNHAEK QKQFEFVGSA PTRRTKRTRR PQPLT 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 murine balb/c 3T3 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 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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FGF-19 is a member of the fibroblast growth factor (FGF) family. After being secreted from the intestine, FGF19 can enter the liver with the circulation and bind to FGFR4 in the liver to act. It has a hormone-like effect and plays an important role in metabolic regulation, such as regulating bile acid metabolism, regulating gallbladder filling, and improving blood glucose. Notably, aberrant expression of FGF19/FGFR4 promotes HCC development and metastasis.   Product Properties Synonyms FGF19;Fibroblast growth factor 1 Uniprot No. O95750 Source Recombinant Human FGF-19 Protein is expressed from HEK293 Cells with Flag tag at the N-terminal. It contains Leu 25-Lys 216. Molecular Weight The protein has a predicted MW of 23.36 kDa. And it migrates as 25-30 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation. Purity > 95% as determined by SDS-PAGE. Biological Activity The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 150 ng/mL. Endotoxin <0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from 0.22 μm filtered solution in PBS (pH 7.4). Reconstitution Centrifuge tubes before opening. Dissolve lyophilized protein with sterile PBS to ensure the concentration is greater than 100 ug/mL.   Shipping and Storage The product should be stored at -25~-15℃ for 1 year from date of receipt. 2-7 days, 2 ~8 °C under sterile conditions after reconstitution. 3 months, -25~-15℃ under sterile conditions after reconstitution. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1.Please operate with lab coats and disposable gloves,for your safety. 2.This product is for research use only.

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Fibroblast growth factor-21 (FGF-21) belongs to the large FGF family which is encoded by the FGF-21 gene. Mature human FGF-21 shows 81% aa identity to mouse FGF-21, and is known to be active on mouse cells. The c-DNA for FGF-21 predicts a 209 aa polypeptide that contains a 28 aa signal sequence and a 181 aa mature region. FGF21 is a metabolic regulator that provides efficient and durable glycemic and lipid control in various animal models. And the FGF21 is a liver-derived endocrine factor that stimulates glucose uptake in adipocytes. Pharmacologic studies show that FGF21 has broad metabolic actions in obese rodents and primates that include enhancing insulin sensitivity, decreasing triglyceride concentrations, and causing weight loss.   Product Properties Synonyms FGF21, FGF-21, fibroblast growth factor 2 Accession Q9NSA1 GeneID 26291 Source E.coli-derived human FGF-21 protein, His29-Ser209 Molecular Weight Approximately 19.4 kDa. AA Sequence HPIPDSSPLL QFGGQVRQRY LYTDDAQQTE AHLEIREDGT VGGAADQSPE SLLQLKALKP GVIQILGVKT SRFLCQRPDG ALYGSLHFDP EACSFRELLL EDGYNVYQSE AHGLPLHLPG NKSPHRDPAP RGPARFLPLP GLPPALPEPP GILAPQPPDV GSSDPLSMVG PSQGRSPSYA S 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 thymidine uptake assay using FGF-receptors transfected BaF3 cells is less than 0.5 μg/ml, corresponding to a specific activity of > 2.0 × 10 3 IU/mg in the presence of 5 µg/ml of recombinant mouse Klotho-β and 10 μg/ml of heparin. 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.   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 IGFs are mitogenic, polypeptide growth factors that stimulate the proliferation and survival of various cell types, including muscle, bone, and cartilage tissue in vitro. IGFs are predominantly produced by the liver, although a variety of tissues produce the IGFs at distinctive times.  The IGFs belong to the Insulin gene family, which also contains insulin and relaxin.  The IGFs are similar to insulin by structure and function, but have a much higher growth-promoting activity than insulin. IGF-II expression is influenced by placenta lactogen, while IGF-I expression is regulated by growth hormone. Both IGF-I and IGF-II signal through the tyrosine kinase type I receptor (IGF-IR), but IGF-II can also signal through the IGF-II/Mannose-6-phosphate receptor. Mature IGFs are generated by proteolytic processing  of  inactive  precursor  proteins,  which  contain  N-terminal  and  C-terminal  propeptide  regions. Recombinant Human IGF-I and IGF-II are globular proteins containing 70 and 67 amino acids, respectively, and 3 intra-molecular disulfide bonds.   Product Properties Synonyms Insulin-like Growth Factor-II, Somatamedin A Accession E3UN46 GeneID 3481 Source E.coli-derived Human IGF-2 protein,Ala25-Glu91. Molecular Weight Approximately 7.5 kDa. AA Sequence AYRPSETLCG GELVDTLQFV CGDRGFYFSR PASRVSRRSR GIVEECCFRS CDLALLETYC ATPAKSE Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 98 % by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using serum free human MCF-7 cells is less than 2 ng/mL, corresponding to a specific activity of > 5.0 × 105 IU/mg. 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 Tris-HCl, pH 8.0, 150 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 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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Fibroblast growth factor 23 (FGF- 23) is a member of the FGF family, within a subfamily that also includes FGF- 19 and FGF- 21. FGF proteins contain a 120 amino acid (aa) core FGF domain that exhibits a beta-trefoil structure. β-Klotho has been identified as co-factor required for FGF-19, 21, 23 signaling. It can obviously increase ligand-receptor affinity. Klotho has a restricted distribution that limits FGF- 23 activity. FGF- 23 is produced by osteocytes and osteoblasts in response to high circulating phosphate levels, elevated parathyroid hormone, and circulatory volume loading. It functions as an endocrine phosphatonin by suppressing circulating phosphate levels. FGF- 23 interaction with renal proximal tubular epithelium decreases the renal resorption of phosphate by down-regulating phosphate transporters and by suppressing vitamin D production. It also decreases the intestinal absorption of phosphate.   Product Properties Synonyms ADHR,HPDR2, HYPF Accession Q9GZV9 GeneID 8074 Source E.coli-derived Human FGF-23, Thr25-Ile227. Molecular Weight Approximately 25.3 kDa. AA Sequence YPNASPLLGS SWGGLIHLYT ATARNSYHLQ IHKNGHVDGA PHQTIYSALM IRSEDAGFVV ITGVMSRRYL CMDFRGNIFG SHYFDPENCR FQHQTLENGY DVYHSPQYHF LVSLGRAKRA FLPGMNPPPY SQFLSRRNEI PLIHFNTPIP RRHTRSAEDD SERDPLNVLK PRARMTPAPA SCSQELPSAE DNSPMASDPL GVVRGGRVNT HAGGTGPEGC RPFAKFI 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 thymidine uptake assay using FGF-receptors transfected BaF3 cells is less than 0.5 μg/mL, corresponding to a specific activity of > 2.0 × 10 3 IU/mg in the presence of 0.3 μg/mL of rMuKlotho and 10 μg/mL of heparin. 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.   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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IGF-BP3 is a 30 kDa, cysteine-rich secreted protein. It is the major IGF binding protein present in the plasma of human and animals, and it is also found in α-granules of platelets. In addition to its ability to modulate the activity of IGF-I and IGF-II, IGF-BP3 exerts inhibitory effects on follicle stimulating hormone (FSH) activity. Decreased plasma levels of IGF-BP3 often results in dwarfism, whereas elevated levels of IGF-BP3 may lead to acromegaly. The expression of IGF-BP3 in fibroblasts is stimulated by mitogenic growth factors, such as Bombesin, Vasopressin, PDGF, and EGF. Recombinant Human IGF-BP3 is a 28.8 kDa protein consisting of 264 amino acid residues.   Product Properties Synonyms Growth-hormone-dependant Binding Protein, IBP-3, IGF-binding protein 3 Accession P17936 GeneID 3486 Source E.coli-derived Human IGF-BP3 protein,Gly28-Lys291 Molecular Weight Approximately 28.8 kDa. AA Sequence GASSAGLGPV VRCEPCDARA LAQCAPPPAV CAELVREPGC GCCLTCALSE GQPCGIYTER CGSGLRCQPS PDEARPLQAL LDGRGLCVNA SAVSRLRAYL LPAPPAPGNA SESEEDRSAG SVESPSVSST HRVSDPKFHP LHSKIIIIKK GHAKDSQRYK VDYESQSTDT QNFSSESKRE TEYGPCRREM EDTLNHLKFL NVLSPRGVHI PNCDKKGFYK KKQCRPSKGR KRGFCWCVDK YGQPLPGYTT KGKEDVHCYS MQSK Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 98 % by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The ED50 as determined by inhibiting IGF-II induced proliferation of serum free human MCF-7 cells is less than 200 ng/mL, corresponding to a specific activity of > 5.0 × 103 IU/mg in the presence of 15 ng/mL of rHuIGF-II. Endotoxin < 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°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 fibroblast growth factor-4 (FGF-4) gene was identified as HST-1 gene from human stomach cancers and Kaposi’ s sarcoma by a NIH3T3 transforming assay. FGF-4 has pleiotropic roles in many cell types and tissues, it is a mitogenic, angiogenic and survival factor, which is involved in cell proliferation and differentiation and in a variety of development processes.   Product Properties Synonyms HST, HST-1, HSTF-1, HBGF-4, Transforming Protein KS3, KFGF Uniprot No. P08620 Source E.coli-derived human FGF-4, Ser54-Leu206. Molecular Weight Approximately 16.8 kDa. Purity > 95% as determined by SDS-PAGE. 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. Reconstitution Centrifuge tubes before opening. Dissolve lyophilized protein with PBS to ensure the concentration is greater than 100ug/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.   Notes 1.Please operate with lab coats and disposable gloves,for your safety. 2.This product is for research use only.

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IGF-BPs control the distribution, function and activity of IGFs in various cell tissues and body fluids. IGF-BP4 is the major IGF-BP produced by osteoblasts, and is found in the epidermis, ovarian follicles,  and other tissues.  IGF-BP4 inhibits the activity  of IGF-I and IGF-II by binding in a manner that results in the formation of complexes with reduced ability to signal through cell surface IGF receptors. IGF-BP4 can inhibit the growth of chick pelvis cartilage and HT29 colon adenocarcinoma  cells  by  blocking  the mitogenic actions of IGFs, and has also been shown to reduce colony formation by colorectal cancer cells via an IGF-independent pathway. The biological effects of IGF-BP4 can be regulated by Pregnancy Associated Plasma Protein A (PAPP-A), which reduces IGF-BP4/IGF binding affinity by proteolytically cleaving IGF-BP4. The modulation of IGF-BP4 activity by  PAPP-A  is  an important component in the regulation of ovarian folliculogenesis and  in  the  growth  inhibition  of  responding  ovarian  cancer cells. Recombinant Human IGF-BP4 is a 25.7 kDa protein consisting of 237 amino acid residues including, the IGF-BP domain and thyroglobulin type-I domain.   Product Properties Synonyms Insulin-like Growth Factor-Binding Protein 4, IBP-4, HT29-IGF-BP, colon cancer cell growth inhibitor Accession P22692 GeneID 3487 Source Insect Cell-derived Human IGF-BP4 protein,Asp22-Glu258. Molecular Weight Approximately 30 kDa. AA Sequence DEAIHCPPCS EEKLARCRPP VGCEELVREP GCGCCATCAL GLGMPCGVYT PRCGSGLRCY PPRGVEKPLH TLMHGQGVCM ELAEIEAIQE SLQPSDKDEG DHPNNSFSPC SAHDRRCLQK HFAKIRDRST SGGKMKVNGA PREDARPVPQ GSCQSELHRA LERLAASQSR THEDLYIIPI PNCDRNGNFH PKQCHPALDG QRGKCWCVDR KTGVKLPGGL EPKGELDCHQ LADSFRE Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97 % by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The ED50 as determined by its ability to inhibit IGF-II induced proliferation of MCF-7 cells is less than 0.1 μg/mL, corresponding to a specific  activity  of > 1.0 × 104 IU/mg in the presence of 14 ng/ml of rHuIGF-II. 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 °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 FGF-9 protein, also known as fibroblast growth factor 9, is a member of the fibroblast growth factor (FGF) family. It functions as a signaling molecule, regulating various cellular processes like cell proliferation, differentiation, and migration. FGF-9 protein plays a vital role in various physiological and pathological processes, making it an important focus of research in the field of molecular biology and medicine.   Product Properties Synonyms FGF9, FGF-9, Glia-activating factor, GAF, glia-activating factor, HBFG-9, HBGF-9 Uniprot No. P31371 Source E.coli-derived human FGF-9 protein, Leu4-Ser208, with C-terminal His tag. Molecular Weight Approximately25.2kDa. Purity > 90% as determined by SDS-PAGE. Endotoxin < 1 EU per 1μg of the protein by the LAL method. Formulation Liquid in PBS，the concentration is 0.3 mg/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.Please operate with lab coats and disposable gloves, for your safety. 2.This product is for research use only.

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IGF-BPs control the distribution, function and activity of IGFs in various cell tissues and body fluids. Currently, there are seven named IGF-BPs that form high affinity complexes with both IGF-I and IGF-II. IGF-BP5 is a 28.6 kDa,  cysteine-rich, secreted  protein produced by vascular smooth muscle cells. It is the major IGF-binding protein present in bone tissue and helps potentiate the action of IGF-I on smooth muscle cells, fibroblasts, and osteoblasts. Data shows that IGFBP-5 acts as a growth inhibitor and pro-apoptotic agent in breast cancer cells. IGFBP-5-overexpressing mice show an increase in neonatal mortality, reduced female fertility, whole-body growth inhibition, and retarded muscle development. Recombinant Human IGF-BP5 is a 28.6 kDa protein consisting of 253 amino acid residues.   Product Properties Synonyms Human IGF-BP5 Accession P24593 GeneID 3488 Source E.coli-derived HumanIGF-BP5 protein,Leu21-Glu272. Molecular Weight Approximately 28.6 kDa. AA Sequence LGSFVHCEPC DEKALSMCPP SPLGCELVKE PGCGCCMTCA LAEGQSCGVY TERCAQGLRC LPRQDEEKPL HALLHGRGVC LNEKSYREQV KIERDSREHE EPTTSEMAEE TYSPKIFRPK HTRISELKAE AVKKDRRKKL TQSKFVGGAE NTAHPRIISA PEMRQESEQG PCRRHMEASL QELKASPRMV PRAVYLPNCD RKGFYKRKQC KPSRGRKRGI CWCVDKYGMK LPGMEYVDGD FQCHTFDSSN VE 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 its ability to inhibit IGF-II induced proliferation of MCF-7 cells is less than 0.4 μg/mL, corresponding to a specific activity of > 2500 IU/mg in the presence of 15 ng/mL of rHuIGF-II. 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 Sodium Citrate, pH 3.0. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.   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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IGF-BPs control the distribution, function and activity of IGFs in various cell tissues and body fluids. Currently, there are seven named IGF-BPs that form high affinity complexes with both IGF-I and IGF-II. IGF-BP7 is expressed in a wide range of normal human tissues, and it generally shows reduced expression in cancer cell lines of prostate, breast, colon, and lung origin.  It plays a  role in skeletal myogenesis by binding to IGF in a manner that inhibits IGF-induced differentiation of skeletal myoblasts, without affecting IGF-induced proliferation. Additionally, IGF-BP7 suppresses growth and colony formation of prostate and breast  cancer cell lines through an IGF-independent mechanism, which causes a delay in the G1 phase of the cell cycle and increased apoptosis. Recombinant Human IGF-BP7 is a 26.4 kDa protein consisting of 256 amino acid residues.   Product Properties Synonyms Insulin-like Growth Factor-Binding Protein 7, IBP-7, Mac25, IGF binding protein related protein-1 (IGFBP-rP1) Accession Q16270 GeneID 3490 Source E.coli-derived HumanIGF-BP7 protein,Leu21-Glu282. Molecular Weight Approximately 26.4 kDa. AA Sequence SSSDTCGPCE PASCPPLPPL GCLLGETRDA CGCCPMCARG EGEPCGGGGA GRGYCAPGME CVKSRKRRKG KAGAAAGGPG VSGVCVCKSR YPVCGSDGTT YPSGCQLRAA SQRAESRGEK AITQVSKGTC EQGPSIVTPP KDIWNVTGAQ VYLSCEVIGI PTPVLIWNKV KRGHYGVQRT ELLPGDRDNL AIQTRGGPEK HEVTGWVLVS PLSKEDAGEY ECHASNSQGQ ASASAKITVV DALHEIPVKK GEGAEL Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95 % 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 8.6, 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.   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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IFNA1, also known as IFN-alpha and IFNA, belongs to the alpha/beta interferon family. Interferons(IFNs) are proteins made and released by host cells in response to the presence of pathogens such as viruses, bacteria, parasites, or tumor cells. They belong to the large class of glycoproteins known as cytokines. Leukocyte interferon is produced predominantly by B lymphocytes. Immune interferon is produced by mitogen- or antigen-stimulated T lymphocytes. IFNA1 is produced by macrophages and has antiviral activities.IFNs stimulate the production of two enzymes: a protein kinase and an oligoadenylate synthetase. They allow for communication between cells to trigger the protective defenses of the immune system that eradicate pathogens or tumors. IFNs can activate immune cells, such as natural killer cells and macrophages; they increase recognition of infection or tumor cells by up-regulating antigen presentation to T lymphocytes, and they also increase the ability of uninfected host cells to resist new infection by the virus.   Product Properties Synonyms IFN-alpha 1a protein Accession P01562 GeneID 3439 Source E.coli-derived Human IFN-α1a protein,Cys24-Glu189. Molecular Weight Approximately 19.5 kDa. AA Sequence MCDLPETHSL DNRRTLMLLA QMSRISPSSC LMDRHDFGFP QEEFDGNQFQ KAPAISVLHE LIQQIFNLFT TKDSSAAWDE DLLDKFCTEL YQQLNDLEAC VMQEERVGET PLMNADSILA VKKYFRRITL YLTEKKYSPC AWEVVRAEIM RSLSLSTNLQ ERLRRKE 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 determined by an anti-viral assay is no less than 1.0 × 108 IU/mg. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered solution in PBS, pH 7.4, containing 3 % Mannitol, 5 % Trehalose, 0.05 % 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 °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 cytokine Fms-like tyrosine kinase 3 ligand (FLT3L), also known as Flt-3 Ligand, is an important regulator of hematopoiesis. Its receptor, Flt3, is expressed on myeloid, lymphoid and dendritic cell progenitors and is considered an important growth and differentiation factor for several hematopoietic lineages. Activating mutations of Flt3 are frequently found in acute myeloid leukemia (AML) patients and associated with a poor clinical prognosis. Mature human Flt- 3L consists of a 158 amino acid (aa) extracellular domain (ECD) with a cytokine-like domain and a juxtamembrane tether region, a 21 aa transmembrane segment, and a 30 aa cytoplasmic tail. At the amino acid sequence level, human and mouse FL are approximately 72% identical and the two proteins exhibit cross-species activity. The Flt3-L manifests antitumor activity, presumably due to its capacity to recruit dendritic cells and cause their proliferation.   Product Properties Synonyms Flt3-Ligand, FL, FLG3L, Flt3L, SL Cytokin Accession P49771 GeneID 2323 Source E.coli-derived human IL-1alpha protein, Thr27-Ala181. Molecular Weight Approximately 17.6 kDa. AA Sequence TQDCSFQHSP ISSDFAVKIR ELSDYLLQDY PVTVASNLQD EELCGGLWRL VLAQRWMERL KTVAGSKMQG LLERVNTEIH FVTKCAFQPP PSCLRFVQTN ISRLLQETSE QLVALKPWIT RQNFSRCLEL QCQPDSSTLP PPWSPRPLEA TAPTA 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 AML5 cells is less than 1.0 ng/mL, corresponding to a specific activity of > 1.0 × 10 6 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 7.0. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions.   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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Interferons (IFN) are a family of cytokines with potent antiviral, antiproliferative and immunomodulatory properties, classified based on their binding specificity to cell surface receptors . Human IFNA2 was originally cloned in the early ‘80s and now more than a dozen closely related IFN alpha subtypes have been identified in both the human and mouse genome, each sharing about 80% amino acid (aa) sequence homology. Structurally, type I IFNs belong to the class of five helical- bundle cytokines, with the IFNA subtypes containing 2 conserved disulfide bonds. The extracellular domain (ECD) of mature human IFNA1, also known as IFNA13, shares 63% aa sequence identity with mouse IFNA1. Two variants of human IFNA1 are known to exist, IFNA1a and IFNA1b, which only differ by a single residue at position 137. The type I IFNs bind to the interferon alpha receptor (IFNAR), which consists of two subunits: IFNAR1 (alpha - subunit) and IFNAR2 (beta - subunit).   Product Properties Synonyms Human IFN-α1b Accession P01562 GeneID 3439 Source E.coli-derived Human IFN-α1b protein,Cys24-Glu189(A115).with an N-terminal Met. Molecular Weight Approximately 19.5 kDa. AA Sequence MCDLPETHSL DNRRTLMLLA QMSRISPSSC LMDRHDFGFP QEEFDGNQFQ KAPAISVLHE LIQQIFNLFT TKDSSAAWDE DLLDKFCTEL YQQLNDLEAC VMQEERVGET PLMNVDSILA VKKYFRRITL YLTEKKYSPC AWEVVRAEIM RSLSLSTNLQ ERLRRKE 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 specific activity determined by an anti-viral assay is no less than 1.0 × 108 IU/mg. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered solution in PBS, pH 7.4, containing 4% mannitol and 1 % HSA. 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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IFNA2 (Interferon Alpha 2) is a Protein Coding gene. This gene is a member of the alpha interferon gene cluster on chromosome 9. The encoded protein is a cytokine produced in response to viral infection. Type I Interferons (IFNs) are well-known cytokines that exert antiviral activity, antitumor activity, and immunomodulatory effects. Interferon tau (IFNT), a type I IFN similar to alpha IFNs(IFNA), is the pregnancy recognition signal produced by the ruminant conceptus. Among the IFN-α genes, a total of 28 different sequence variants have been described. The three principal subtypes of IFNα-2 are designated α-2a, α-2b, and α-2c. IFNα-2b is being the predominant allele while IFNα-2a is less predominant and IFNα-2c only a minor allelic variant.   Product Properties Synonyms IFN-alpha 2a protein Accession P01563 GeneID 3440 Source Yeast-derived Human IFN-α2a protein,Cys24-Glu188. Molecular Weight Approximately 19.2 kDa. AA Sequence CDLPQTHSLG SRRTLMLLAQ MRKISLFSCL KDRHDFGFPQ EEFGNQFQKA ETIPVLHEMI QQIFNLFSTK DSSAAWDETL LDKFYTELYQ QLNDLEACVI QGVGVTETPL MKEDSILAVR KYFQRITLYL KEKKYSPCAW EVVRAEIMRS FSLSTNLQES LRSKE 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 determined by an anti-viral assay is no less than 1.0 × 108 IU/mg. Endotoxin < 1 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 °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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Follistatin (FS) was initially identified as a follicle-stimulating hormone inhibiting substance found in ovarian follicular fluid. It has since been shown that FS is a high‑affinity activin-binding protein that can act as an activin antagonist. Two alternatively spliced follistatin mRNAs, encoding mature FS with 288 amino acid (aa) residues (FS‑288) and 315 aa residues (FS‑315), exist. Natural FS purified from porcine ovaries is primarily a carboxy-terminal truncated form of FS‑315 composed of 300 aa residues. Cell surface-associated FS has been suggested to play a role in the clearance and bioavailability of activin in vivo. Besides activin, FS has also been shown to bind with multiple BMPs and to inhibit BMP activity in early Xenopus embryos. FS deficient mice have been shown to have multiple embryonic defects that will result in death shortly after birth. Product Properties Synonyms FS; FSActivin-binding protein; FST Accession P19883 GeneID 10468 Source E.coli-derived Human Follistatin, Gly30-Asn317. Molecular Weight Approximately 31.5 kDa. AA Sequence GNCWLRQAKN GRCQVLYKTE LSKEECCSTG RLSTSWTEEDVNDNTLFKWM IFNGGAPNCI PCKETCENVD CGPGKKCRMN KKNKPRCVCA PDCSNITWKG PVCGLDGKTY RNECALLKAR CKEQPELEVQ YQGRCKKTCR DVFCPGSSTC VVDQTNNAYC VTCNRICPEP ASSEQYLCGN DGVTYSSACH LRKATCLLGR SIGLAYEGKC IKAKSCEDIQ CTGGKKCLWD FKVGRGRCSL CDELCPDSKS DEPVCASDNA TYASECAMKE AACSSGVLLE VKHSGSCN Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95% 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 mm filtered concentrated solution in 20mM Tris-HCl, pH 8.5, 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.   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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IFNA2 (Interferon Alpha 2) is a Protein Coding gene. This gene is a member of the alpha interferon gene cluster on chromosome 9. The encoded protein is a cytokine produced in response to viral infection. Type I Interferons (IFNs) are well-known cytokines that exert antiviral activity, antitumor activity, and immunomodulatory effects. Interferon tau (IFNT), a type I IFN similar to alpha IFNs(IFNA), is the pregnancy recognition signal produced by the ruminant conceptus. Among the IFN-α genes, a total of 28 different sequence variants have been described. The three principal subtypes of IFNα-2 are designated α-2a, α-2b, and α-2c. IFNα-2b is being the predominant allele while IFNα-2a is less predominant and IFNα-2c only a minor allelic variant.   Product Properties Synonyms IFN-alpha 2b protein Accession P01563 GeneID 3440 Source Yeast-derived Human IFN-α2a protein, Cys24-Glu188(K23R). Molecular Weight Approximately 19.2 kDa. AA Sequence CDLPQTHSLG SRRTLMLLAQ MRKISLFSCL KDRHDFGFPQ EEFGNQFQKA ETIPVLHEMI QQIFNLFSTK DSSAAWDETL LDKFYTELYQ QLNDLEACVI QGVGVTETPL MKEDSILAVR KYFQRITLYL KEKKYSPCAW EVVRAEIMRS FSLSTNLQES LRSKE 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 specific activity determined by an anti-viral assay is no less than 1.6 × 108 IU/mg. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered solution in PBS, pH 7.4, with 0.02 % Tween-20 Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.   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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CX3CL1, also named neurotactin, is a novel chemokine identified through bioinformatics. CX3CL1 has a unique C-X3-C cysteine motif near the amino-terminus and is the first member of a fourth branch of the chemokine superfamily. Unlike other known chemokines, CX3CL1 is a type 1 membrane protein containing a chemokine domain tethered on a long mucin-like stalk. The extracellular domain of human CX3CL1 can be released, possibly by proteolysis at the dibasic cleavage site proximal to the membrane, to generate soluble CX3CL1. CX3CL1 mRNA has been detected in various tissues including the brain and heart. The expression of CX3CL1 was also reported to be up-regulated in endothelial cells and microglia by inflammatory signals. Membrane-bound CX3CL1 has been shown to promote adhesion of leukocytes. The soluble chemokine domain of human CX3CL1 was reported to be chemotactic for T cells and monocytes while the soluble chemokine domain of mouse CX3CL1 was reported to chemoattract neutrophils and T-lymphocytes but not monocytes. The gene for human CX3CL1 has been mapped to chromosome 16q. Product Properties Synonyms C-X3-C motif chemokine 1, CX3C membrane-anchored chemokine, Neurotactin, Small-inducible cytokine D1 Accession P78423 GeneID 6376 Source E.coli-derived Human Fractalkine/CX3CL1, Gln25-Gly100. Molecular Weight Approximately 8.6 kDa. AA Sequence QHHGVTKCNI TCSKMTSKIP VALLIHYQQN QASCGKRAII LETRQHRLFC ADPKEQWVKD AMQHLDRQAA ALTRNG Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97% by SDS-PAGE and HPLC analyses. Biological Activity The biological activity determined by a chemotaxis bioassay using human T-lymphocytes is in a concentration of 5.0-10 ng/mL. Fully biologically active when compared to standard. Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM PB, pH 7.4, 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.   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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Interferon-alpha (IFN-alpha), also known as leukocyte interferon, represents a group of related but distinct proteins that share over 95% amino acid sequence homology. They are members of the type I interferon family which share a common cell surface receptor composed of two subunits, a 100 kDa ligand-binding subunit (IFN-alpha R2) and a 125 kDa ligand binding and signal transduction subunit (IFN-alpha R1) that is involved both in ligand binding and signal transduction. IFN-alpha has both anti-viral and immunomodulatory activities on target cells.   Product Properties Synonyms IFN-α2c Source Yeast-derived Human IFN-α2c protein,Cys24-Glu188(K23R,H24R. Molecular Weight Approximately 19.3 kDa. AA Sequence CDLPQTHSLG SRRTLMLLAQ MRRISLFSCL KDRRDFGFPQ EEFGNQFQKA ETIPVLHEMI QQIFNLFSTK DSSAAWDETL LDKFYTELYQ QLNDLEACVI QGVGVTETPL MKEDSILAVR KYFQRITLYL KEKKYSPCAW EVVRAEIMRS FSLSTNLQES LRSKE 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 activity is determined by the cytopathic effect inhibition assay. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered solution in PBS, pH 7.4, with 0.02 % Tween-20. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.   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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IFN λ1, 2, and 3 (also known as IL-29, IL-28A and IL-28B respectively) are distantly related to the  IL-10  family  and  the interferons. All three IFN-lambdas use a distinct receptor system composed of an IFN-λR1 subunit (also called CRF2-12) and IL-10R2 subunit (also called CRF2-14). Signaling through this receptor system induces antiviral defenses similar to, but distinct from, that of type I interferons. Recombinant Human IFN-λ1 is a 19.8 kDa protein containing 178 amino acid residues.   Product Properties Synonyms Cytokine Zcyto21 Accession Q8IU54 GeneID 282618 Source E.coli-derived Human IFN-λ1 protein,Gly20-Thr200. Molecular Weight Approximately 19.8 kDa. AA Sequence GPVPTSKPTT TGKGCHIGRF KSLSPQELAS FKKARDALEE SLKLKNWSCS SPVFPGNWDL RLLQVRERPV ALEAELALTL KVLEAAAGPA LEDVLDQPLH TLHHILSQLQ ACIQPQPTAG PRPRGRLHHW LHRLQEAPKK ESAGCLEASV TFNLFRLLTR DLKYVADGNL CLRTSTHPES T 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 an anti-viral assay using human HepG2 cells infected with encephalomyocarditis is less than 5 ng/mL, corresponding to a specific activity of > 2.0 × 105 IU/mg. Endotoxin < 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 °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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CXCL1, also known as KC, GRO alpha, and CINC-1, is an approximately 8 kDaproinflammatorychemokine that plays a key role in neutrophil migration and activation. Mature human CXCL1 shares 64% and 67% aa sequence identity with mouse and rat CXCL1, respectively. It is produced by many cell types in inflammatory sites and during chronic inflammatory diseases. CXCL1 can associate into bioactive dimers and primarily signals through CXCR2/IL-8 RB but can also bind with lower affinity to CXCR2/IL-8 RA. It induces neutrophil migration, extravasation, respiratory burst, and degranulation and also induces T cells to produce proinflammatory IL-17. CXCL1 additionally binds to Syndecan-1 on epithelial cells which acts as a sink for CXCL1 activity until Syndecan-1 cleavage by MMP-7. CXCL1 is up-regulated in spinal cord astrocytes by inflammatory stimuli or tumor cell injection, and it exacerbates pain sensation by potentiating excitatory NMDA neurotransmission. In the circulatory system, CXCL1 interacts with CXCR2 on endothelial cells to promote lymphatic tube formation and angiogenesis . It promotes the hypertrophic differentiation of chondrocytes resulting in cartilage matrix deposition, calcification, and remodeling. It interacts with both CXCR1 and CXCR2 on adipose stromal cells and promotes their recruitment to prostate tumors in obese patients.. It also binds CXCR2 on ovarian cancer cells, leading to cleavage of cell surface HB-EGF, transactivation of EGFR, and cell proliferation.     Product Properties Synonyms GROα, MGSA, NAP-3 Accession P09341 GeneID 2919 Source E.coli-derived Human GRO-α,Ala35-Asn107. Molecular Weight Approximately 7.9 kDa AA Sequence ASVATELRCQ CLQTLQGIHP KNIQSVNVKS PGPHCAQTEV IATLKNGRKA CLNPASPIVK KIIEKMLNSD KSN 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 peripheral blood neutrophils is in a concentration range of 10-50 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, 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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GCP-2 (granulocyte chemotactic protein-2) also known as CXCL6, is a CXC chemokine initially isolated as a neutrophil chemoattractant from the MG-63 osteosarcoma cell line. Among human CXC chemokines, GCP-2 is most closely related to ENA-78 (78% amino acid (aa) sequence identity in the mature peptide region and 86% identity in the signal sequence). The structure and sequence of the genes for human GCP-2 and ENA-78 also exhibit close similarity suggesting the two genes may have originated from a gene duplication. LIX (LPS-induced CXC chemokine) was initially cloned as a gene induced by LPS in mouse fibroblasts. The predicted LIX protein sequence is identical to a previously purified mouse protein designated mouse GCP-2 based on its amino sequence similarity (60% sequence identity) to human GCP-2. Mouse GCP-2/LIX is also 54% identical with human ENA-78 at the amino acid sequence level.     Product Properties Synonyms Human GCP-2/CXCL6 Accession P80162 GeneID 6372 Source E.coli-derived Human CXCL6,Val43-Val114. Molecular Weight Approximately 7.9 kDa AA Sequence VLTELRCTCL RVTLRVNPKT IGKLQVFPAG PQCSKVEVVA SLKNGKQVCL DPEAPFLKKV IQKILDSGNK KN Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 98 % by SDS-PAGE and HPLC analyses. Biological Activity Fully biologically active when compared to standard. The biological activity determined by a chemotaxis bioassay using human peripheral blood neutrophils is in a concentration range of 10-50 ng/mL. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in Acetonitrile and TFA Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.   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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GM-CSF (Granulocyte-Macrophage Colony-Stimulating Factor) is a cytokine that belongs to the colony-stimulating factor family.It plays an important role in immunomodulation, hematopoiesis and inflammation.GM-CSF is mainly produced by a variety of cells, including macrophages, T cells, B cells and fibroblasts.It is produced by a variety of cells, including macrophages, T cells, B cells and fibroblasts. It can stimulate the proliferation, differentiation and functional activation of granulocytes and monocytes in the hematopoietic cell lineage.GM-CSF can promote the differentiation of pluripotent stem cells in the bone marrow to granulocytes and monocytes, increase the number of leukocytes, and improve their function, thus enhancing the body's immune response and anti-infection ability. In addition, GM-CSF has an important role in regulating the activation of macrophages and dendritic cells and anti-microbial activity. In clinical practice, GM-CSF is widely used in the treatment of bone marrow transplantation-related complications, malignant tumors, and immunodeficiency. It is also used as a tool in laboratory studies to explore the regulatory mechanisms of the hematopoietic and immune systems and to develop new therapeutic strategies.This recombinant human GM-CSF is supplied as a lyophilized powder with high activity, high purity, low endotoxin, and no redundant labeling.   Product Properties Synonyms Granulocyte/Macrophage Colony-Stimulating Factor, GM-CSF, CSF-2, MGI-1GM, Accession P04141 Source E.coli-derived human GM-CSF protein, Ala18-Glu144. Molecular Weight Approximately 14.5 kDa AA Sequence APARSPSPST QPWEHVNAIQ EARRLLNLSR DTAAEMNETV EVISEMFDLQEPTCLQTRLE LYKQGLRGSL TKLKGPLTMM ASHYKQHCPP TPETSCATQI ITFESFKENL KDFLLVIPFD CWEPVQE 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 0.1 ng/mL, corresponding to a specific activity of>1.0 x 107 lU/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 °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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(C-X-C motif) ligand (CXCL)10 (CXCL10), also known as IP-10, belongs to the ELR(-) CXC subfamily chemokine. CXCL10 was originally identified as an IFN-gamma -inducible gene in monocytes, fibroblasts and endothelial cells. It has since been shown that CXCL10 mRNA is also induced by LPS, IL-1 beta, TNF- alpha, IL-12 and viruses. CXCL10 was originally identified as an IFN-gamma -inducible gene in monocytes, fibroblasts and endothelial cells. CXCL10/IP-10 exerts its function through binding to chemokine (C-X-C motif) receptor 3 (CXCR3), a seven trans-membrane receptor coupled to G proteins. CXCL10/IP-10 and its receptor, CXCR3, appear to contribute to the pathogenesis of many autoimmune diseases, organ specific (such as type 1 diabetes, autoimmune thyroiditis, Graves' disease and ophthalmopathy), or systemic (such as rheumatoid arthritis, psoriatic arthritis, systemic lupus erythematosus, mixed cryoglobulinemia, Sjögren syndrome, or systemic sclerosis). In adition, CXCL10 has been reported to be a potent inhibitor of angiogenesis and to display a potent thymus-dependent antitumor effect.     Product Properties Synonyms Gamma-IP10, Small-inducible Cytokine B10 Accession P02778 GeneID 3627 Source E.coli-derived Human IP-10/CXCL10, Val22-Pro98. Molecular Weight Approximately 8.6 kDa AA Sequence VPLSRTVRCT CISISNQPVN PRSLEKLEII PASQFCPRVE IIATMKKKGE KRCLNPESKA IKNLLKAVSK EMSKRSP 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 peripheral blood neutrophils is in a concentration range 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 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.   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 hedgehog (hh) gene encoding a secreted protein was originally identified in Drosophila as a segment polarity gene. The vertebrate homologues of Hh comprise several proteins including sonic hedgehog (Shh), Indian hedgehog (Ihh), and Desert hedgehog (Dhh). Hedgehog proteins are important signaling molecules during embryonic development and are highly conserved within and across species. Mouse and human Ihh share 100% amino acid identity in the signaling domain, while mouse Ihh and Shh share 90% amino acid identity in the N-terminal signaling domain. Ihh mRNA expression is detected in fetal lung, gut, stomach, liver, kidney, pancreas and strongly in cartilage - in growth regions of the developing bone. Ihh, along with parathyroid hormone related protein, regulate the rate of chondrocyte proliferation and differentiation. Ihh is also involved in yolk sac vasculogenesis, playing an important role in differentiation of epiblast cells into endothelial and red blood cells.Mouse Ihh cDNA encodes a 411 amino acid (aa) polypeptide with a predicted 27 aa signal peptide. This polypeptide is cleaved to generate a 45 kDa precursor protein that undergoes the same post‑translation processing as Shh. An autocatalytic reaction yields a 19 kDa amino‑terminal domain Ihh‑N protein that retains all known signaling capabilities, and a 23 kDa carboxy‑terminal domain Ihh-C protein. Since hydrophobic modifications to Shh, including the substitution of the N-terminal cysteine residue with two hydrophobic isoleucine residues, can also increase its potency, a similar modification was made for Ihh. This modified form also shows increased potency in a bioassay measuring induction of alkaline phosphatase. At the cell surface, Hedgehog activity is mediated by a multicomponent receptor complex involving the 12‑pass transmembrane protein Patched (Ptc) which binds Hedgehogs with high affinity and Smoothened (Smo), a signaling seven transmembrane G-protein coupled receptor.     Product Properties Synonyms HHG-2 Accession Q14623 GeneID 3549 Source E.coli-derived Human IHH C28II, Cys28-Gly202. Molecular Weight Approximately 19.8 kDa AA Sequence IIGPGRVVGS RRRPPRKLVP LAYKQFSPNV PEKTLGASGR YEGKIARSSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDRLNSLAI SVMNQWPGVK LRVTEGWDED GHHSEESLHY EGRAVDITTS DRDRNKYGLL ARLAVEAGFD WVYYESKAHV HCSVKSEHSAAAKTGG 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 its ability to induce alkaline phosphatase production by C3H10T1/2(CCL-226) cells is 3.0-10 μg/mL. Fully biologically active when compared to standard Endotoxin < 1.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 1 × PBS, pH 7.4. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.   Shipping and Storage The products are shipped with ice pack and can be stored at -20℃ to -80℃ for 1 year. Recommend to aliquot the protein into smaller quantities when first used and avoid repeated freeze-thaw cycles.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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All three isoforms of GRO are CXC chemokines that can signal through the CXCR1 or CXCR2 receptors. The GRO proteins chemoattract and activate neutrophils and basophils. Recombinant Human GRO-β is a 7.9 kDa protein consisting of 73 amino acids, including the 'ELR' motif common to the CXC chemokine family that binds to CXCR1 or CXCR2.     Product Properties Synonyms MIP2-alpha Accession P19875 GeneID 2920 Source E.coli-derived Human GRO-β Ala35-Asn107 Molecular Weight Approximately 7.9 kDa. AA Sequence APLATELRCQ CLQTLQGIHL KNIQSVKVKS PGPHCAQTEV IATLKNGQKA CLNPASPMVK KIIEKMLKNG KSN 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 CXCR2 transfected human 293 cells is in a concentration range of 10-100 ng/mL. Endotoxin < 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 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.   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 GRO alpha, GRO beta (MIP-2 alpha ), and GRO gamma (MIP-2 beta ) are products of three distinct, non-allelic human genes. GRO beta and GRO gamma share 90% and 86% amino acid sequence homology, respectively, with GRO alpha. All three human GROs are members of the alpha (C-X-C) subfamily of chemokines and are thought to be the homologs of murine KC and MIP-2. The three GRO cDNAs encode 107 amino acid precursor proteins from which the N-terminal 34 amino acid residues are cleaved to generate the mature GROs. There are no potential N-linked glycosylation sites in the amino acid sequences. GRO expression is inducible by serum or PDGF and/or by a variety of inflammatory mediators, such as IL-1 and TNF, in monocytes, fibroblasts, melanocytes and epithelial cells. In certain tumor cell lines, GRO is expressed constitutively. Similar to other alpha chemokines, the three GRO proteins are potent neutrophil attractants and activators. In addition, these chemokines are also active toward basophils. All three GROs can bind with high affinity to the IL-8 receptor type B.   Product Properties Synonyms GRO-gamma, MIP2-beta Accession P19876 GeneID 2921 Source E.coli-derived Human GRO-γ Ala35-Asn107 Molecular Weight Approximately 7.9 kDa. AA Sequence ASVVTELRCQ CLQTLQGIHL KNIQSVNVRS PGPHCAQTEV IATLKNGKKA CLNPASPMVQ KIIEKILNKG STN 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 CXCR2 transfected human 293 cells is in a concentration range of 10-100 ng/mL. Endotoxin < 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 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.   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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CCL1, also known as I-309 or TCA-3, is a member of the chemokine (C-C motif) ligand family. Human CCL1 was initially identified by subtractive hybridization as a transcript that was present in a gamma /δ T cell line but not in EBV-transformed B cells. CCL1 cDNA encodes a 96 amino acid residue precursor protein with a hydrophobic signal peptide that is cleaved to yield a 73 amino acid residue mature protein. CCL1 interacts with the G protein-linked transmembrane chemokine receptors CCR8 and induces biochemical events that may result in the control of chemotaxis, proliferation, apoptosis and adhesion. It has been demonstrated that CCL1 displays chemotactic activity for monocytes and other cell types such as NK cells and dendritic cells, but not for neutrophils. Furthermore, as the only known physiological ligand for CCR8, CCL1 was identified as a potent inhibitor of HIV-1 envelope-mediated cell-cell fusion and virus infection. CCL1 induces significant levels of LTC4 from elicited eosinophils.   Product Properties Synonyms Small-inducible cytokine A1, T lymphocyte-secreted protein I-309 Accession P22362 GeneID 634 Source E.coli-derived Human I-309/CCL1, Ser23-Lys96. Molecular Weight Approximately 8.6 kDa. AA Sequence SKSMQVPFSR CCFSFAEQEI PLRAILCYRN TSSICSNEGL IFKLKRGKEA CALDTVGWVQ RHRKMLRHCP SKRK Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97 % by SDS-PAGE and HPLC analyses. Biological Activity The biological activity determined by a chemotaxis bioassay using human T-lymphocytes is in a concentration range of 10-100 ng/mL. Fully biologically active when compared to standard. Endotoxin < 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 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 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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Growth Differentiation Factor-7 (GDF-7; also called BMP-12 and CDMP-3) is a member of the BMP family of TGF-beta superfamily proteins. GDF-7 is synthesized as a large precursor protein that consists of an N--terminal 19 amino acid (aa) signal sequence, a 302 aa pro region and a 129 aa C-terminal mature peptide. At the amino acid level, mature human GDF-7 shares 85% and 88% aa sequence identity with mature GDF-7 in mouse and rat, respectively. Mature human GDF-7 lacks a glycine repeat that is found in both mouse and rat GDF-7. Based on sequence similarity, GDF-7 is categorized with GDF-5 and -6, as a subgroup within the BMP family. GDF-7 functions as a homodimer and elicits its bioactivity by mediating the formation of a heterodimeric receptor complex consisting of a type 1 (BMPR-IB) and a type II (BMPR-II or Activin RII) serine/threonine kinase receptor. GDF-7 signaling  results in the phosphorylation and activation of cytosolic Smad proteins (Smad1, 5, and 8).   Product Properties Synonyms BMP12，GDF7 Accession Q7Z4P GeneID 151449 Source E.coli-derived Human GDF-7/BMP-12, Thr322-Arg450. Molecular Weight Approximately 28.0 kDa. AA Sequence TALAGTRTAQ GSGGGAGRGH GRRGRSRCSR KPLHVDFKEL GWDDWIIAPL DYEAYHCEGL CDFPLRSHLE PTNHAIIQTL LNSMAPDAAP ASCCVPARLS PISILYIDAA NNVVYKQYED MVVEACGCR 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 inducing alkaline phosphatase production of murine ATDC5 cells is less than 1.0 μg/mL, corresponding to a specific activity of > 1000 IU/mg. Fully biologically active when compared to standard. Endotoxin < 1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered 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 °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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Regulation of GDF6 expression seems to be a mechanism for evolving species-specific changes in skeletal structures. Seems to positively regulate differentiation of chondrogenic tissue through the growth factor receptors subunits BMPR1A, BMPR1B, BMPR2 and ACVR2A, leading to the activation of SMAD1-SMAD5-SMAD8 complex. The regulation of chondrogenic differentiation is inhibited by NOG. Also involved in the induction of adipogenesis from mesenchymal stem cells. This mechanism acts through the growth factor receptors subunits BMPR1A, BMPR2 and ACVR2A and the activation of SMAD1-SMAD5-SMAD8 complex and MAPK14/p38.   Product Properties Synonyms BMP13, GDF1 Accession Q6KF1 GeneID 39225 Source E.coli-derived Human GDF-6/BMP-13, Thr336-Arg455. Molecular Weight Approximately 27.1 kDa. AA Sequence TAFASRHGKR HGKKSRLRCS KKPLHVNFKE LGWDDWIIAP LEYEAYHCEG VCDFPLRSHL EPTNHAIIQT LMNSMDPGST PPSCCVPTKL TPISILYIDA GNNVVYKQYE DMVVESCGCR 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 inducing alkaline phosphatase production of murine ATDC5 cells is less than 2.0 μg/mL, corresponding to a specific activity of > 500 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 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 °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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Growth Differentiation Factor-5 (GDF-5; also called BMP-14 and CDMP-1) is a member of the BMP family of TGF-beta superfamily proteins. Human GDF-5, -6, and -7 are a defined subgroup of the BMP family. GDF-5 is synthesized as a homodimeric precursor protein consisting of a 354 amino acid (aa) N-terminal pro-region and a 120 aa C-terminal mature peptide. Mature human GDF-5 shares 99% aa sequence identity with both mature mouse and rat GDF-5. GDF-5 signaling is mediated by formation of a heterodimeric complex consisting of a type 1 (BMPR-IB) and a type II (BMPR-II or Activin RII) serine/threonine kinase receptor which results in the phosphorylation and activation of cytosolic Smad proteins (Smad1, 5, and 8). Similar to other BMP family proteins, GDF-5 signaling is antagonized by Noggin. GDF-5 is involved in multiple developmental processes including limb generation, cartilage development, joint formation, bone morphogenesis, cell survival, and neuritogenesis.   Product Properties Synonyms CDMP-1, CDMP1LAP4 Accession P43026 GeneID 8200 Source E.coli-derived Human GDF-5/BMP-14, Ala382-Arg501. Molecular Weight Approximately 27.1 kDa. AA Sequence APLATRQGKR PSKNLKARCS RKALHVNFKD MGWDDWIIAP LEYEAFHCEG LCEFPLRSHL EPTNHAVIQT LMNSMDPEST PPTCCVPTRL SPISILFIDS ANNVVYKQYE DMVVESCGCR 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 inducing alkaline phosphatase production of murine ATDC5 cells is less than 1.0 μg/mL, corresponding to a specific activity of > 1000 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 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 °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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GDNF is a disulfide-linked homodimeric neurotrophic factor that is a potent growth factor for dopamine and motor neurons and is structurally related to Artemin, Neurturin, and Persephin.GDNF signals through a multicomponent receptor system consisting of RET and one of the four GFRα (α1-α4) receptors.GDNF specifically promotes dopamine uptake and survival, as well as morphological differentiation of midbrain neurons. In a mouse model of Parkinson's disease, GDNF improves bradykinesia, rigidity and postural instability.This recombinant mouse GDNF is supplied as a lyophilized powder with high activity, high purity, low endotoxin, and no redundant labeling.   Product Properties Synonyms Astrocyte-derived trophic factor, ATF, ATF-1, ATF2, GDNF, HFB1-GDNF, HGDNF, HSCR3 Accession P39905 Source E.coli-derived Human GDNF protein, Ser78-Ile211. Molecular Weight Approximately 31.1 kDa. AA Sequence SPDKQMAVLP RRERNRQAAA ANPENSRGKG RRGQRGKNRG CVLTAIHLNV TDLGLGYETK EELIFRYCSG SCDAAETTYD KILKNLSRNR RLVSDKVGQA CCR PIAFDDD LSFLDDNLVY HILRKHSAKR CGCI 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 rat C6 cells is less than 0.1 ng/ml,corresponding to a specific activity of > 5.0×107 IU/mg. 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 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 °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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IGF-1, also known as insulin-like growth factor 1, is a protein that plays a crucial role in growth and development. It is produced mainly by the liver and other tissues in response to growth hormone secretion. IGF-1 is a vital protein in human physiology, contributing to growth, development, and maintenance of various tissues and metabolic processes.   Product Properties Synonyms IGF-I, IGF1A, somatomedin C, MGF Accession P05019-1 Source E.coli-derived Human  IGF-1 protein, Gly49-Ala118, with C-terminal Flag tag. Molecular Weight Approximately 8.6 kDa. Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 90 % by SDS-PAGE  analyses. Biological Activity Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using serum free human MCF-7 cells is less than 1 ng/ml,corresponding to a specific activity of > 1.0×106 IU/mg. Endotoxin < 1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered solution in PBS. 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 product should be stored at -25~-15℃ for 1 year from date of receipt. 2-7 days, 2 ~8 °C under sterile conditions after reconstitution. 3 months, -25~-15℃ under sterile conditions after reconstitution.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Galectin-1, a polypeptidic factor that can have major effects on cell growth and apoptosis, is an important regulator of leukocyte function and tumor angiogenesis. Galectin-1 belongs to a family of 15 structurally related β-galactoside binding proteins that are able to control a variety of cellular events, including cell cycle regulation, adhesion, proliferation, and apoptosis. Human Galectin-1 shares 88% aa sequence identity with mouse, equine and ovine, 90% with rat, and 87% with bovine and porcine  Galectin-1. Recombinant human galectin-1 to three porphyrin compounds: Zn-porphyrin (ZnTPPS); Mn-porphyrin and Au-porphyrin. These compounds are widely applied in the photodynamic therapy of cancer. Galectin-1 can also modulate cell-cell and cell-matrix interactions.   Product Properties Synonyms Beta-galactoside-binding lectin L-14-I, BHL, DKFZp686E23103, GAL1, gal-1, Galaptin, galectin 1, Galectin1, Galectin-1, GBP, HBL, HLBP14, HPL, L-14, Lactose-binding lectin 1, LGALS1 Accession P09382 Source E.coli-derived Human Galectin-1, Ala2-Asp135. Molecular Weight Approximately 14.6 kDa. Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95% by SDS-PAGE  analyses. Biological Activity The biological activity determined by a chemotaxis bioassay using human blood monocytes is in a concentration range of 1.0-10 ng/mL. Fully biologically active when compared to standard. Endotoxin < 0.1 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered solution in PBS, pH 7.4, with 1 mM DTT. 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 -25~-15℃ for 1 year. 1 months, 2 ~8℃ under sterile conditions after reconstitution.  3 months, -25 ~ -15℃ under sterile conditions after reconstitution.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Galectin-3, is classified as a chimeric member of the Galectin superfamily. Nuclear Galectin-3 can modulate gene expression, while cytosolic Galectin-3 can inhibit apoptosis. Galectin-3 contributes to the innate immune response against Candida albicans and Streptococcus pneumoniae, and it can facilitate acute inflammatory responses via neutrophil activation and opsonization, macrophage recruitment, and mast cell activation.   Product Properties Synonyms AGE-R3, CBP35, GAL3, L29, LGALS3, Mac-2 Accession P17931 Source Yeast-derived Human Galectin-3, Ala2-Ile250. Molecular Weight Approximately 26.0 kDa. Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 90% by SDS-PAGE  analyses. Biological Activity Recombinant human Galectin-3 is able to agglutinate red blood cells at a minimumeffective concentration of 25ug/ml. 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, 1%BSA. Reconstitution 1. We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom.Reconstitute in sterile PBS, pH 7.4, with 0.1% BSA to a concentration of 0.1-1.0 mg/mL. 2. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in PBS, which must contain carrier proteins, such as 0.1% BSA, 10% FBS, 5% HSA, 5% trehalose, one of four options.   Shipping and Storage The products are shipped with ice pack and can be stored at -25~-15℃ for 1 year. 1 months, 2 ~8℃ under sterile conditions after reconstitution.  3 months, -25 ~ -15℃ under sterile conditions after reconstitution.   Cautions 1. Avoid repeated freeze-thaw cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Growth hormone (GH), also known as somatotropin, is a member of a family of growth factors that includes prolactin, placental lactogens, proliferins, and somatolactin. It is synthesized primarily by somatotropes in the anterior pituitary and is stored in secretary granules. The pulsatile release of GH into circulation is regulated by the concerted actions of the hypothalamic hormones - GH-releasing hormone (GHRH) and somatostatin (SST) - as well as by signals from the periphery - ghrelin and leptin . GH stimulates the liver and other tissues to produce IGF-1, which regulates growth and metabolism. GH has also been shown to have direct effects on growth that is independent of IGF-1. GH, directly or indirectly via IGF-1, can act on B cells, T cells, NK cells, macrophages and neutrophils to exert immunomodulatory activities. Futhermore, GH can act directly on various cell types to induce lipolysis, lactation, amino acid uptake and protein synthesis. Product Properties Synonyms GH1, GH, GHN, GH-N, hGH-N, Pituitary Growth Hormone, Growth Hormone 1, Somatotropin Accession P01241 Source E.coli-derived Human GH, Phe27-Phe217. Molecular Weight Approximately 22 kDa. 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 rat Nb2-11 lymphoma cells is less than 0.1 ng/ml, corresponding to a specific activity of > 1.0 × 107 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 20 mM PB, pH 7.0, with 3% Mannitol. 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 -25~-15℃ 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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G-CSF is a hematopoietic growth factor that stimulates the development of progenitor cells that transform to neutrophils and enhances the functional activity of mature terminal cells.G-CSF is produced in response to specific stimulation of a variety of cells, including macrophages, fibroblasts, endothelial cells, and the bone marrow stroma.G-CSF is used clinically to promote hematopoietic recovery after bone marrow transplantation.G-CSF is used clinically to promote hematopoietic recovery after bone marrow transplantation. This recombinant human G-CSF is supplied as a lyophilized powder with high activity, high purity, low endotoxin, and no redundant labeling.   Product Properties Synonyms G-CSF, CSF-3, MGI-1G, GM-CSF beta, MGC45931,Pluripoietin Accession P09919 Source E.coli-derived Human G-CSF protein, Thr31-Pro204. Molecular Weight Approximately 18.9 kDa. AA Sequence TPLGPASSLP QSFLLKCLEQ VRKIQGDGAA LQEKLCATYK LCHPEELVLL GHSLGIPWAP LSSCPSQALQ LAGCLSQLHS GLFLYQGLLQ ALEGISPELG PTLDTLQLDV ADFATTIWQQ MEELGMAPAL QPTQGAMPAF ASAFQRRAGG VLVASHLQSF LEVSYRVLRH LAQP 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 mouse NFS-60 cells is less than 0.05 ng/mL, corresponding to a specific activity of>2.0 x 107 lU/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 10 mM Sodium Citrate, pH 4.0, 150 mM NaCl, 0.01% Tween-20.   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 HB-EGF (Heparin-Binding EGF-like growth factor), also known as the DTR (diphtheria toxin receptor), is a 12-16 kDa member of the EGF family of peptide growth factors. It is further classified as a group 2 ErbB ligand based on its ability to activate both the EGF/ErbB1 and ErbB4 receptors. Mature HB-EGF is a soluble peptide that arises from proteolytic processing of the transmembrane form. The transmembrane form of HBEGF is a juxtacrine growth and adhesion factor and is uniquely the receptor for diphtheria toxin. Cells known to express HB-EGF include bronchial epithelium, visceral and vascular smooth muscle , CD4+ T cells, cardiac muscle, glomerular podocytes, keratinocytes and IL-10-secreting regulatory macrophages. HBEGF participates in diverse biological processes, including heart development and maintenance, skin wound healing, eyelid formation, blastocyst implantation, the progression of atherosclerosis, and tumor formation, through the activation of signaling molecules downstream of ErbB receptors and interactions with molecules associated with HBEGF. tumor necrosis factor-alpha (TNF-alpha) and interleukin-1 beta markedly increased HB-EGF mRNA levels in HUVEC by 12- and 7-fold, respectively, and induction of the gene by TNF-alpha was both dose- and time-dependent.   Product Properties Synonyms HBEGF, DT-R Accession P99075 Source E.coli-derived Human HB-EGF, Asp63-Leu148. Molecular Weight Approximately 9.7 kDa. AA Sequence DLQEADLDLL RVTLSSKPQA LATPNKEEHG KRKKKGKGLG KKRDPCLRKY KDFCIHGECK YVKELRAPSC ICHPGYHGER CHGLSL Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97 % by SDS-PAGE and HPLC analyses. Biological Activity The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 1 ng/mL, corresponding to a specific activity of>1.0 x 106 lU/mg.Fully biologically active when compared to standard. Endotoxin < 01.0 EU per 1μg of the protein by the LAL method. Formulation Lyophilized from a 0.2 µm filtered solution in  20 mM PB, pH 7.4, 130 mM NaCl. Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 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 CCL14 is belonging to the CC chemokine family. It has two isoforms, CCL14a (HCC-1) and CCL14b (HCC-3). The sequence of HCC-3 differs from HCC-1 as follow: 27-27 R → QTGGKPKVVKIQLKLVG. CCL14 was first isolated from the hemofiltrate of human patients with chronic renal failure. CCL14 promotes chemotaxis of T lymphocytes, monocytes and eosinophils, and inhibits infection of M-tropic human immunodeficiency virus type 1 and is a ligand for CCR1, CCR3 and CCR5. CCL14 is expressed constitutively in several normal tissues: spleen, liver, skeletal and heart muscle, gut, and bone marrow, present at high concentrations in plasma.   Product Properties Synonyms CC-1 Protein, Human; CC-3 Protein, Human; CKB1 Protein, Human; FLJ16015 Protein, Human; HCC-1 Protein, Human; HCC-1(1-74) Protein, Human; HCC-1/HCC-3 Protein, Human; HCC-3 Protein, Human; MCIF Protein, Human; NCC-2 Protein, Human; NCC2 Protein, Human; SCYA14 Protein, Human; SCYL2 Protein, Human; SY14 Protein, Human Accession Q16627 Source E.coli-derived Human Hemofiltrate CC Chemokine-1 Protein, Thr22-Asn93 Molecular Weight Approximately 8.4 kDa. AA Sequence TESSSRGPYH PSECCFTYTT YKIPRQRIMD YYETNSQCSK PGIVFITKRG HSVCTNPSDK WVQDYIKDMK EN 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 5.0-20 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, 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 cycles. 2. For your safety and health, please wear lab coats and disposable gloves for operation. 3. For research use only!

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Interleukin-18 (IL-18), also known as IL-1F4, is a proinflammatory cytokine that belongs to the IL-1 superfamily and is produced by macrophages and other cells. It is expressed as a 24 kDa precursor by endothelial and epithelial cells, keratinocytes, gamma δ T cells, and phagocytes. Mature human IL-18 shares approximately 63% amino acid sequence identity with mouse and rat IL-18. IL-18 activation is induced by infection or tissue damage and leads to disease pathology in chronic inflammation. In the presence of IL-12 or IL-15, IL-18 enhances anti-viral Th1 immune responses by inducing IFN-gamma production and the cytolytic activity of CD8+ T cells and NK cells. IL-18 induces the antigen-independent production of IL-17 by gamma δ T cells and CD4+ T cells. IL-18 also promotes myeloid dendritic cell maturation and triggers neutrophil respiratory burst. In the absence of IL-12 or IL-15, IL-18 promotes production of the Th2 cytokines IL-4 and IL-13 by CD4+ T cells and basophils. IL-18 induces the antigen-independent production of IL-17 by gamma δ T cells and CD4+ T cells. IL-18 also promotes myeloid dendritic cell maturation and triggers neutrophil respiratory burst. In cancer, IL-18 has shown a variety of activities, including enhancing anti-tumor immunity, inhibiting or promoting angiogenesis, and promoting tumor cell metastasis.   Product Properties Synonyms IL-1F4 Accession Q14116 GeneID 3606 Source E.coli-derived Human IL-11, Tyr37-Asp193. Molecular Weight Approximately 18.2 kDa. AA Sequence YFGKLESKLS VIRNLNDQVL FIDQGNRPLF EDMTDSDCRD NAPRTIFIIS MYKDSQPRGM AVTISVKCEK ISTLSCENKI ISFKEMNPPD NIKDTKSDII FFQRSVPGHD NKMQFESSSY EGYFLACEKE RDLFKLILKK EDELGDRSIM FTVQNED Tag None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 95% by SDS-PAGE analyses. Biological Activity Test in processing. Endotoxin Less than 0.1 EU/μg of rHuIL-18 as determined by LAL method. Formulation Lyophilized from a 0.2 μm filtered solution in PBS, pH 7.0. Reconstitution 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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Interleukin 7 (IL-7) is a cytokine involved in the regulation of immune cell development and survival, including T and B lymphocytes. It is produced by stromal cells, such as fibroblasts and bone marrow stromal cells. Dysregulation of IL-7 signaling has been implicated in autoimmune diseases and cancer.   Product Properties Synonyms Interleukin 7;IL7; IL-7; IL-7interleukin-7; interleukin 7; Lymphopoietin-1; PBGF Uniprot No. P13232 Source Recombinant Human IL-7 Protein is expressed from HEK293 Cells . It contains Asp 26-His 177. Molecular Weight The protein has a predicted MW of 19.34 kDa. And it migrates as 25-33 kDa under reducing (R)condition (SDS-PAGE) due to glycosylation. Purity > 95% as determined by SDS-PAGE. Endotoxin <0.1 EU per 1μg of the protein by the LAL method Formulation Lyophilized from 0.22 μm filtered solution in PBS (pH 7.4) Reconstitution Centrifuge tubes before opening. Dissolve lyophilized protein with sterile PBS to ensure the concentration is greaterthan 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.Please operate with lab coats and disposable gloves,for your safety. 2.This product is for research use only.

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Interleukin-8 (IL-8), also known as CXCL8, GCP-1, and NAP-1, is a widely expressed proinflammatory member of the CXC family of chemokines. This chemokine is secreted by a variety of cell types including monocyte/macrophages, T cells, neutrophils, fibroblasts, endothelial cells, and various tumor cell lines in response to inflammatory stimuli (IL1, TNF, LPS, etc). IL-8/CXCL8 can associate into a homodimer or a heterodimer with CXCL4/PF4 (2), and it can interact with matrix and cell surface glycosaminoglycans. Near its N-terminus, this 8-9 kDa chemokine contains an ELR motif which is important for its angiogenic properties. Numerous observations have established IL-8/CXCL8 as a key mediator in neutrophil-mediated acute inflammation due to its potent actions on neutrophils. In addition, IL-8/CXCL8 has crucial roles in various pathological conditions such as chronic inflammation and cancer. It induces VEGF expression, vascular endothelial cell proliferation, angiogenesis, and tumor cell invasiveness.   Product Properties Synonyms (Ser-IL-8)72, GCP/IL-8 protein I, IL8/NAP1 form III, LYNAP, MDNCF-c, NA Accession P10145 GeneID 3576 Source E.coli-derived Human IL-8,72aa/CXCL8, Ser28-Ser99 AA Sequence SAKELRCQCI KTYSKPFHPK FIKELRVIES GPHCANTEII VKLSDGRELC LDPKENWVQR VVEKFLKRAE NS Tag  None Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder. Purity > 97% by SDS-PAGE and HPLC analyses. Biological Activity less than 2 ng/mL, corresponding to a specific activity of > 5.0 × 10 5 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.   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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