Biolegend, 570756, Biotinylated Recombinant Human VEGFR2-Fc Chimera (carrier-free)

The VEGF family includes five members, VEGFA, VEGFB, VEGFC, VEGFD, and placenta growth factor (PlGF). Structurally, these growth factors are homodimers, although heterodimers have been described that are composed of VEGFA and PIGS. There are three VEGF receptor tyrosine kinases: VEGFR1 (Flt1), VEGFR2 (KDR/Flk1), and VEGFR3 (Flt4). VEGFR1 is expressed on monocytes and macrophages, VEGFR2 on vascular endothelial cells, and VEGFR3 on lymphatic endothelial cells. VEGFR2 binds to proteolytically processed VEGFC and VEGFD. VEGFR2 is the major mediator of the signaling cascades that regulate endothelial cell functions including proliferation, migration and differentiation. Soluble VEGFR2 was initially identified in mouse and human plasma resulting from an endothelial cell surface proteolytic cleavage. VEGFA stimulates ADAM17- dependent shedding of VEGFR2. In addition, its shedding is stimulated by phorbol ester (PMA) and the calcium ionophore, ionomycin. Soluble VEGFR1 and VEGFR2 act as decoy receptors for VEGFA regulating the availability of VEGFA. Upon ligand binding, VEGFR1 and VEGFR2 can dimerize as homodimers or heterodimers, contributing to various pathways and downstream effects. In addition, alternative splicing of VEGFR2 produces soluble VEGFR2 that binds VEGFC and subsequently prevents lymphangiogenesis. It has been reported that decreased levels of VEGFR2 in the plasma of preeclamptic women may serve as a marker of endothelial cell dysfunction.