VEGFR-3/FLT4 Protein, Human (HEK293, His-Avi)

VEGFR-2 protein is a tyrosine-protein kinase receptor that plays a crucial role in regulating various processes including angiogenesis, vascular development, vascular permeability, and embryonic hematopoiesis. It acts as a cell-surface receptor for VEGFA, VEGFC, and VEGFD, promoting the proliferation, survival, migration, and differentiation of endothelial cells. Additionally, isoforms lacking a transmembrane domain, such as isoform 2, act as decoy receptors for VEGFA, VEGFC, and/or VEGFD, serving as negative regulators of lymphangiogenesis by inhibiting the binding of these growth factors to FLT4. VEGFR-2 also forms heterodimers with FLT1 and FLT4, modulating their signaling. Activation of isoform 1 by vascular growth factors triggers multiple signaling cascades, including the activation of PLCG1, resulting in the production of diacylglycerol and inositol 1,4,5-trisphosphate, as well as the activation of protein kinase C. It also activates MAPK1/ERK2, MAPK3/ERK1, and AKT1 signaling pathways, leading to various cellular responses. Moreover, VEGFR-2 phosphorylates PIK3R1, facilitating the activation of phosphatidylinositol 3-kinase, and promotes actin cytoskeleton reorganization and activation of PTK2/FAK1. Its role in NOS2 and NOS3 induction leads to the production of nitric oxide (NO) by endothelial cells. Additionally, VEGFR-2 phosphorylates PLCG1 and promotes phosphorylation of FYN, NCK1, NOS3, PIK3R1, PTK2/FAK1, and SRC, further contributing to its diverse cellular functions.