Vascular endothelial growth factor (VEGF or VEGF-A), 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. Different isoforms can be generated by differential splicing (e.g. VEGF165). 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. 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-A with high affinity. In vitro, VEGF is a potent endothelial cell mitogen. The antibody is against the N-terminus and will recognize all VEGF-A isoforms.
