VEGF-165 Human Recombinant Protein
Purity was determined to be greater than 95% as de
Vascular endothelial growth factor A-165, VEGF-A165 cytokine, Vascular permeability factor, VPF-165
Vascular endothelial growth factor-A was originally isolated from tumor cells and referred to as Tumor Angiogenesis Factor or Vascular Permeability Factor. Although expressed at high levels in certain tumor-derived cells it is produced by a wide variety of cell types. In addition to stimulating vascular growth and vascular permeability it may play a role in stimulating vasolidation via nitric oxide-dependent pathways. Alternative splicing of the mRNA for VEGF-A results in several isoforms of the protein being produced. Rat and bovine VEGF are one amino acid shorter than the human factor, and the bovine and human sequences show a homology of 95 percent. In contrast to other factors mitogenic for endothelial cells such as FGF-1, FGF-2 and PDGF, VEGF is synthesized as a precursor containing a typical hydrophobic secretory signal sequence of 26 amino acids. Glycosylation is not required for efficient secretion of VEGF. Recombinant Human VEGF produced in E.coli is a double, non-glycosylated, polypeptide chain containing 165 amino acids and having a molecular mass of 38231 Daltons. VEGF-165 Recombinant Protein has been tested by SDS-PAGE and is suitable as a control for polyclonal or monoclonal anti-VEGF-165 in immunological assays.
