VEGF is a potent mitogen in embryonic and somatic angiogenesis with specificity for vascular endothelial cells. VEGF forms homodimers and exists in four different isoforms. Overall, the VEGF monomer resembles that of PDGF, but its N-terminal segment is helical rather than extended. VEGF shares homologies of about 21% and 24% respectively with the A and B chains of human platelet-derived growth factor (PDGF), and has complete conservation of the eight cysteine residues found in both mature PDGF chains. The cysteine knot motif is a common feature of this domain. The homology is not reflected in function, however, since the cell types responsive to VEGF are distinct from those responsive to homo- and heterodimers of the PDGF chains. This protein is a glycosylated mitogen that acts on endothelial cells and has various effects, including mediating increased vascular permeability, inducing angiogenesis, vasculogenesis and endothelial cell growth, promoting cell migration, and inhibiting apoptosis. VEGF-A also has been shown to have effects on a number of other cell types (e.g. stimulation of monocyte/macrophage migration, neurons, cancer cells, kidney epithelial cells ). VEGF-A is also a vasodilator; it increases microvascular permeability, and was originally referred to as vascular permeability factor. Alternatively spliced transcript variants, encoding either freely secreted or cell-associated isoforms, have been characterized.
This protein-A purified antibody was prepared from whole rabbit serum produced by repeated immunizations with a recombinant protein raised in yeast, corresponding to the 164 amino acids of the mature bovine VEGF-A protein.