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1594 résultats pour « Peprotech »

"Peprotech"

1594 Résultats
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Human IFN-γ Standard TMB ELISA Development Kit, PeproTech, Inc.

Supplier: Peprotech

PeproTech's Human IFN-γ ELISA development kit contains the key components required for the quantitative measurement of natural and/or recombinant human IFN-γ in a sandwich ELISA format.

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Human MCP-1 (CCL2) Standard TMB ELISA Development Kit, PeproTech

Supplier: Peprotech

PeproTech's Human MCP-1 (CCL2) ELISA development kit contains the key components required for the quantitative measurement of natural and/or recombinant human MCP-1 (CCL2) in a sandwich ELISA format.

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Human SCF Standard TMB ELISA Development Kit, PeproTech

Supplier: Peprotech

PeproTech's Human SCF ELISA development kit contains the key components required for the quantitative measurement of natural and/or recombinant human SCF in a sandwich ELISA format.

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Human MIP-1β (CCL4) Standard TMB ELISA Development Kit, PeproTech

Supplier: Peprotech

PeproTech's Human MIP-1β (CCL4) ELISA development kit contains the key components required for the quantitative measurement of natural and/or recombinant human MIP-1β (CCL4) in a sandwich ELISA format.

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Murine IL-4 Standard TMB ELISA Development Kit, PeproTech

Supplier: Peprotech

PeproTech's Murine IL-4 ELISA development kit contains the key components required for the quantitative measurement of natural and/or recombinant murine IL-4 in a sandwich ELISA format.

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Murine IL-6 Standard TMB ELISA Development Kit, PeproTech

Supplier: Peprotech

PeproTech's Murine IL-6 ELISA development kit contains the key components required for the quantitative measurement of natural and/or recombinant murine IL-6 in a sandwich ELISA format.

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Murine TNF-α Standard TMB ELISA Development Kit, PeproTech

Supplier: Peprotech

PeproTech's Murine TNF-α ELISA development kit contains the key components required for the quantitative measurement of natural and/or recombinant mTNF-α in a sandwich ELISA format.

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Human IL-12 Standard TMB ELISA Development Kit, PeproTech, Inc.

Supplier: Peprotech

PeproTech's Human IL-12 ELISA development kit contains the key components required for the quantitative measurement of natural and/or recombinant human IL-12 in a sandwich ELISA format.

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Murine IL-12 Standard TMB ELISA Development Kit, PeproTech

Supplier: Peprotech

PeproTech's Murine IL-12 ELISA development kit contains the key components required for the quantitative measurement of natural and/or recombinant murine IL-12 in a sandwich ELISA format.

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Murine IFN-γ Standard TMB ELISA Development Kit, PeproTech

Supplier: Peprotech

PeproTech's Murine IFN-γ ELISA development kit contains the key components required for the quantitative measurement of natural and/or recombinant murine IFN-γ in a sandwich ELISA format.

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Murine IL-2 Standard TMB ELISA Development Kit, PeproTech

Supplier: Peprotech

PeproTech's Murine IL-2 ELISA development kit contains the key components required for the quantitative measurement of natural and/or recombinant murine IL-2 in a sandwich ELISA format.

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Human IL-17E Standard TMB ELISA Development Kit, PeproTech, Inc.

Supplier: Peprotech

PeproTech's Human IL-17E ELISA development kit contains the key components required for the quantitative measurement of natural and/or recombinant human IL-17E in a sandwich ELISA format.

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Human Recombinant IGF-I (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-I is 7.6 kDa.

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Human Recombinant IGF-I (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. IGF-I LR3 is a recombinant analog of human IGF-I comprised of the complete IGF-I sequence, with an Arginine substitution for the third position Glutamic acid, and a 13 amino acid length N terminus peptide extension. Specifically engineered for higher biological potency Recombinant Human IGF-I LR3 is a 9.1 kDa, single, non-glycosylated polypeptide chain containing 83 amino acid residues.

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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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Human Recombinant PDGF-AA (from E. coli)

Supplier: Peprotech

PDGFs are disulfide-linked dimers consisting of two 12.0-13.5 kDa polypeptide chains, designated PDGF-A and PDGF-B chains. The three naturally occurring PDGFs, PDGF-AA, PDGF-BB and PDGF-AB, are potent mitogens for a variety of cell types, including smooth muscle cells, connective tissue cells, bone and cartilage cells, and some blood cells. The PDGFs are stored in platelet α-granules, and are released upon platelet activation. The PDGFs are involved in a number of biological processes, including hyperplasia, chemotaxis, embryonic neuron development, and respiratory tubule epithelial cell development. Two distinct signaling receptors used by PDGFs have been identified and named PDGFR-α and PDGFR-β. PDGFR-α is high-affinity receptor for each of the three PDGF forms. On the other hand, PDGFR-β interacts with only PDGF-BB and PDGF-AB. Recombinant Human PDGF-AA is a 28.5 kDa disulfide-linked homodimer of two α chains (250 total amino acids).

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