VEGFR-2 Protein, Mouse (HEK293, His, solution)

VEGFR-2, a tyrosine-protein kinase, serves as a crucial cell-surface receptor for VEGFA, VEGFC, and VEGFD, playing a fundamental role in angiogenesis regulation, vascular development, permeability, and embryonic hematopoiesis. It actively promotes endothelial cell proliferation, survival, migration, and differentiation, as well as the reorganization of the actin cytoskeleton. Isoforms lacking a transmembrane domain, like isoform 2, may function as decoy receptors, particularly in negatively regulating VEGFA- and VEGFC-mediated lymphangiogenesis by limiting the availability of free VEGFA and/or VEGFC and preventing their binding to FLT4. VEGFR-2 modulates FLT1 and FLT4 signaling through heterodimer formation. The binding of vascular growth factors to isoform 1 initiates various signaling cascades, including the activation of PLCG1, resulting in the production of diacylglycerol and inositol 1,4,5-trisphosphate and the activation of protein kinase C. Additionally, it mediates the activation of MAPK1/ERK2, MAPK3/ERK1, AKT1, and the phosphorylation of PIK3R1, contributing to phosphatidylinositol 3-kinase regulation and actin cytoskeleton reorganization. VEGFR-2 is indispensable for VEGFA-induced NOS2 and NOS3 expression, leading to nitric oxide production by endothelial cells, and it phosphorylates PLCG1, FYN, NCK1, NOS3, PIK3R1, PTK2/FAK1, and SRC.