Phospho-VEGF Receptor 2 (Y1175) Recombinant Rabbit mAb (S-M0024)

Phospho-VEGF Receptor 2 (Y1175) is the activated form of vascular endothelial growth factor receptor 2 (VEGFR2) phosphorylated at tyrosine residue 1175, and this event represents a core hallmark of VEGF signaling pathway activation. VEGFR2 is a receptor tyrosine kinase primarily expressed on vascular endothelial cells; upon binding to its ligand VEGF-A, the receptor undergoes dimerization and transphosphorylation, among which Y1175 is located within the intracellular kinase insert domain (KID) and is one of the earliest and most important autophosphorylation sites following receptor activation. Phosphorylation at this site recruits SH2 domain-containing adaptor proteins such as phospholipase Cγ (PLCγ), VARP, and Sck/ShcB, thereby initiating multiple downstream key signaling cascades. Among these, the PLCγ-Ca²⁺-eNOS pathway regulates vascular permeability and nitric oxide production, while the Ras-Raf-MEK-ERK pathway activated through adaptor proteins such as Shc primarily drives endothelial cell proliferation, migration, and survival. Therefore, Phospho-VEGFR2 (Y1175) not only serves as a reliable molecular marker for assessing VEGFR2 kinase activity but also represents a core node regulating angiogenesis, vascular remodeling, and vascular barrier function. In oncology, aberrant hyperphosphorylation at this site is frequently closely associated with tumor neovascularization, invasion, metastasis, and resistance to anti-VEGF targeted therapies, making the Y1175 site an important research and monitoring target for evaluating the efficacy of anti-angiogenic drugs and developing novel intervention strategies.