VEGF 165 組換え体(リコンビナント)タンパク質 | Recombinant Human VEGF 165

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• CF(Carrier-Free)とは？
• Product Details
• Additional Information
• Citations

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CF(Carrier-Free)とは？

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Product Details

Source

Spodoptera frugiperda, Sf 21 (baculovirus)-derived, Ala27-Arg191

Accession

NP_001165097

Structure

Disulfide-linked homodimer

Purity

>97%, by SDS-PAGE with silver staining.

Predicted Molecular Mass

19.2 kDa (monomer)

SDS-PAGE

20-22 kDa, reducing conditions39-42 kDa, non-reducing conditions

Activity

Measured in a cell proliferation assay using HUVEC human umbilical vein endothelial cells.Conn, G. et al. (1990) Proc. Natl. Acad. Sci. USA 87

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Additional Information

Molecule Information

VEGF

Aliases

VAS; Vasculotropin; VEGFA; VPF

Entrez Gene IDs

7422 (Human); 22339 (Mouse); 83785 (Rat); 403802 (Canine); 493845 (Feline); 30682 (Zebrafish)

Background

VEGF

Vascular endothelial growth factor (VEGF), also known as vascular permeability factor (VPF) or vasculotropin, is a homodimeric 34 - 42 kDa, heparin-binding glycoprotein with potent angiogenic, mitogenic and vascular permeability-enhancing activities specific for endothelial cells. The amino acid sequence of VEGF exhibits primary structural, as well as limited amino acid sequence, homology with that of the A and B chains of PDGF. All eight cysteine residues involved in intra- and inter-chain disulfide bonds are conserved among these growth factors. A cDNA encoding a protein having a 53% amino acid sequence homology in the PDGF-like region of VEGF has been isolated from a human placental cDNA library. This protein, named placenta growth factor (PlGF), is now recognized to be a member of the VEGF family of growth factors. Based on its homology with VEGF, PlGF was also proposed to be an angiogenic factor. Two receptor tyrosine kinases have been described as putative VEGF receptors. Flt-1 (fms-like tyrosine kinase), and KDR (kinase-insert-domain-containing receptor) proteins have been shown to bind VEGF with high affinity.In vitro, VEGF is a potent endothelial cell mitogen. In cultured endothelial cells, VEGF can activate phospholipase C and induce rapid increases of free cytosolic Ca2+. VEGF has been shown to stimulate von Willebrand factor release from endothelial cells and induce expression of tissue factor activity in endothelial cells as well as in monocytes. VEGF has also been shown to be chemotactic for monocytes and osteoblasts. In vivo, VEGF can induce angiogenesis as well as increase microvascular permeability. As a vascular permeability factor, VEGF acts directly on the endothelium and does not degranulate mast cells. It promotes extravasation of plasma fibrinogen, leading to fibrin deposition which alters the tumor extracellular matrix. The modified extracellular matrix subsequently promotes the migration of macrophages, fibroblasts and endothelial cells. Based on its in vitro and in vivo properties, VEGF is expected to play important roles in inflammation and during normal and pathological angiogenesis, a process that is associated with wound healing, embryonic development, and growth and metastasis of solid tumors. Elevated levels of VEGF have been reported in synovial fluids of rheumatoid arthritis patients and in sera from cancer patients.

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Citations

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