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1594 résultats pour « Peprotech »

"Peprotech"

1594 Résultats
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Anti-TPO Goat Polyclonal Antibody (Biotin)

Supplier: Peprotech

Produced from sera of goats immunized with highly pure Recombinant Human TPO. Anti­Human TPO­specific antibody was purified by affinity chromatography and then biotinylated.

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Human Recombinant FGF-basic (from E. coli), PeproTech

Supplier: Peprotech

FGF-basic is one of 23 known members of the FGF family. Proteins of this family play a central role during prenatal development, postnatal growth and regeneration of a variety of tissues, by promoting cellular proliferation and differentiation. FGF-basic is a non-glycosylated, heparin-binding growth factor that is expressed in the brain, pituitary, kidney, retina, bone, testis, adrenal gland, liver, monocytes, epithelial cells and endothelial cells. FGF-basic signals through FGFR 1b, 1c, 2c, 3c and 4. Recombinant Human FGF-basic is a 16.4 kDa protein consisting of 146 amino acid residues.

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Human Recombinant VEGF-D (from HEK293 Cells)

Supplier: Peprotech

VEGF-D, a member of the VEGF/PDGF family of structurally related proteins, is a potent angiogenic cytokine. It promotes endothelial cell growth, promotes lymphangiogesis, and can also affect vascular permeability. VEGF-D is highly expressed in the lung, heart, small intestine and fetal lung, and at lower levels in the skeletal muscle, colon, and pancreas. It forms cell surface-associated, non-covalent, disulfide-linked homodimers, and can bind and activate both VEGFR-2 (flk1) and VEGFR-3 (flt4) receptors. During embryogenesis, VEGF-D may play a role in the formation of the venous and lymphatic vascular systems. It also participates in the growth and maintenance of differentiated lymphatic endothelium in adults. Both VEGF-C and VEGF-D are over-expressed in certain cancers, and the resulting elevated levels of VEGF-C or VEGF-D tend to correlate with increased lymphatic metastasis. Recombinant Human VEGF-D is a 26.2 kDa, non-disulfide linked, homodimeric protein consisting of two 117 amino acid polypeptide chains. Due to glycosylation, the protein migrates as a 20.0-22.0 kDa band by SDS-PAGE analysis under non-reducing conditions.

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Mouse Recombinant KC (from E. coli)

Supplier: Peprotech

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 Murine KC (CXCL1) is a 7.8 kDa protein consisting of 72 amino acids, including the 'ELR' motif common to the CXC chemokine family that binds to CXCR1 or CXCR2.

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Mouse Recombinant IL-17A (from E. coli)

Supplier: Peprotech

The originally described IL-17 protein, now known as IL-17A, is a homodimer of two 136 amino acid chains that are secreted by activated T-cells, which act on stromal cells to induce production of proinflammatory and hematopoietic bioactive molecules. Today, IL-17 represents a family of structurally-related cytokines that share a highly conserved C-terminal region, but differ from one another in their N-terminal regions and in their distinct biological roles. The six known members of this family, IL-17A through IL-17F, are secreted as homodimers. IL-17A exhibits cross-species bioactivity between human and murine cells. Recombinant Murine IL-17A is a 30.0 kDa, disulfide-linked homodimer of two 133 amino acid, polypeptide chains.

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Human Recombinant IL-17F (from E. coli)

Supplier: Peprotech

IL-17F, a member of the IL-17 family of structurally related cytokines, has been shown to stimulate the proliferation and activation of T-cells and PBMCs. IL-17F also regulates cartilage matrix turnover and inhibits angiogenesis. The mature human IL-17F is a homodimeric protein with a total weight of 30.1 kDa, consisting of two 133 amino acid residue chains.

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Mouse Recombinant IL-10 (from E. coli)

Supplier: Peprotech

IL-10 is an immunosuppressive cytokine produced by a variety of mammalian cell types including macrophages, monocytes, T cells, B cells and keratinocytes. IL-10 inhibits the expression of proinflammatory cytokines such as IL-1 and TNF-alpha. Like IL-4, IL-10 enhances humoral immune responses and attenuates cell-mediated immune reactions. Human IL-10 is active on murine cells, but murine IL-10 is inactive on human cells. Recombinant Murine IL-10 is an 18.7 kDa protein of 161 amino acid residues.

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Human Recombinant IL-15 (from E. coli)

Supplier: Peprotech

IL-15 is an immunomodulating cytokine that stimulates the proliferation of T lymphocytes and shares many biological properties with IL-2. IL-15 exerts its biological activities primarily on T cells. It is also essential in the development, survival and activation of NK cells. Increased expression of IL-15 has been linked to with rheumatoid arthritis, inflammatory bowel disease, and diseases affiliated with retroviruses HIV and HTLV-I. Human IL-15 is biologically active on mouse cells as measured by the dose-dependent stimulation of the proliferation of mouse CTLL cells. Recombinant Human IL-15 is a 12.9 kDa protein consisting of 115 amino acid residues.

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Human Recombinant ANGPTL-3 (from CHO cells)

Supplier: Peprotech

ANGPTL-3 (Angiopoietin-like protein 3) is a member of the angiopoietin family of structurally related proteins, characterized by a coiled N-terminal domain and a C-terminal fibrinogen-like domain. It is primarily expressed in the liver, and can exert activities related to both angiogenesis and lipid metabolism. ANGPTL-3 inhibits lipoprotein lipase (LPL) and endothelial lipase (EL), which has the effect of increasing plasma levels of triglycerides and HDL-associated cholesterol. The fibrinogen-like portion of the ANGPTL-3 protein can bind alpha-5/beta-3 integrins, leading to endothelial cell adhesion and migration. Recombinant Human ANGPTL-3 is a glycoprotein that migrates by SDS-PAGE analysis at an apparent molecular weight of 62 kDa, and contains 452 amino acid residues including a C-terminal His tag. The calculated molecular weight of Recombinant Human ANGPTL-3 is 52.9 kDa.

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Anti-IL-1beta Rabbit Polyclonal Antibody

Supplier: Peprotech

Produced from sera of rabbits immunized with highly pure Recombinant Rat IL-1β. Anti­Rat IL-1β­specific antibody was purified by affinity chromatography employing an immobilized Rat IL-1β matrix.

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Anti-IL-15 Rabbit Polyclonal Antibody

Supplier: Peprotech

Produced from sera of rabbits immunized with highly pure Recombinant Human IL-15. Anti­Human IL-15­specific antibody was purified by affinity chromatography employing an immobilized Human IL-15 matrix.

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Anti-AITRL Rabbit Polyclonal Antibody (Biotin)

Supplier: Peprotech

Produced from sera of rabbits immunized with highly pure Recombinant Human AITRL. Anti­Human AITRL­specific antibody was purified by affinity chromatography and then biotinylated.

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Human Recombinant IGF-II (from E. coli)

Supplier: Peprotech

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. The calculated molecular weight of Recombinant Human IGF-II is 7.5 kDa.

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Mouse Recombinant GDNF (from E. coli)

Supplier: Peprotech

GDNF is a disulfide-linked, homodimeric neurotrophic factor structurally related to Artemin, Neurturin and Persephin. These proteins belong to the cysteine-knot superfamily of growth factors that assume stable dimeric protein structures. GDNF signals through a multicomponent receptor system, composed of a RET and one of the four GFRα (α1-α4) receptors. GDNF specifically promotes dopamine uptake and survival, and morphological differentiation of midbrain neurons. Using a Parkinson’s disease mouse model, GDNF has been shown to improve conditions such as bradykinesia, rigidity, and postural instability. The functional murine GDNF ligand is a disulfide-linked homodimer consisting of two 15.1 kDa polypeptide chains called monomers. Each monomer contains seven conserved cysteine residues, including Cys-101, which is used for inter-chain disulfide bridging, and others that are involved in the intramolecular ring formation known as the cysteine knot configuration. The calculated molecular weight of Recombinant Murine GDNF is 30.2 kDa.

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Mouse Recombinant RANTES (from E. coli)

Supplier: Peprotech

RANTES is a CC chemokine that can signal through the CCR1, CCR3, CCR5 and US28 (cytomegalovirus receptor) receptors. It is a chemoattractant towards monocytes, memory T cells (CD4+/CD45RO), basophils, and eosinophils. RANTES also has the capability to inhibit certain strains of HIV-1, HIV-2 and simian immunodeficiency virus (SIV). Recombinant Murine RANTES (CCL5) is a 7.8 kDa protein containing 68 amino acid residues, including the four highly conserved cysteine residues present in the CC chemokines.

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Human Recombinant Follistatin (from E. coli), PeproTech

Supplier: Peprotech

Follistatin is a secreted protein that binds to ligands of the TGF-β family and regulates their activity by inhibiting their access to signaling receptors. It was originally discovered as an activin antagonist whose activity suppresses expression and secretion of the pituitary hormone FSH (follicle stimulating hormone). In addition to being a natural antagonist, follistatin can inhibit the activity of other TGF-β ligands including BMP-2,-4,-6,-7, Myostatin, GDF-11, and TGF-β1. Follistatin is expressed in the pituitary, ovaries, decidual cells of the endometrium, and in some other tissues. Recombinant Human Follistatin is a 31.5 kDa protein containing 288 amino acids. Its primary structure contains three cysteine-rich domains (called FS domains), each followed by a protease-inhibitory kazal domain.

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