human VEGF189 protein Human 5 µg

Human Vascular Endothelial Growth Factor VEGF189, a 21 kDa protein consisting of 189 amino acid residues, is produced as a homodimer. VEGF is a polypeptide growth factor and a member of the platelet-derived growth factor family. It is a specific mitogen for vascular endothelial cells and a strong angiogenic factor in vivo. Two high-affinity tyrosine kinase receptors for VEGF165 have been identified, VEGFR-1 (FLT-1), and VEGFR-2 (KDR). Consistent with the endothelial cell-specific action of VEGF165, expression of both receptor genes has been found predominantly but not exclusively on endothelial cells. Expression of VEGFR-1 was also found on human monocytes, neutrophils (PMNs), bovine brain pericytes and villous and extravillous trophoblasts. In addition to its action as a mitogen it is a potent vascular permeability factor (VPF) in vivo. VEGF165 is also a chemoattractant molecule for monocytes and endothelial cells. 5 different proteins are generated by differential splicing: VEGF121, VEGF145, VEGF165, VEGF189 and VEGF206. The most abundant form is VEGF165. Whereas VEGF121 and VEGF165 are secreted proteins, VEGF145, VEGF189 and VEGF206 are strongly cell-associated. The isoforms VEGF145, VEGF165 and VEGF189 bind to heparin with high affinity. VEGF165 is apparently a homodimer, but preparations of VEGF165 show some heterogeneity on SDS gels, depending on the secretion of different glycosylation patterns. All dimeric forms have similar biological activities but their bioavailability is very different. There is good evidence that there also exist heterodimeric molecules between the different isoforms and that different cells and tissues express different VEGF isoforms. The other members of this increasing growth factor family are VEGF-B, -C, -D and -E. Another member is the Placenta growth factor PlGF.