VEGFR-2/KDR (D7), soluble

Recombinant Human soluble Endothelial Growth Factor Receptor-2 (sKDR (D7) ) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein consists of all 7 extracellular domains, which contain all the information necessary for high affinity ligand binding. The receptor monomers have a mass of approximately 116 kDa. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs) . They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4) . Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signaling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. The binding of VEGF165 to VEGFR-2 is dependent on heparin.