Phospho-VEGF Receptor 2 (Tyr1175) Recombinant Rabbit mAb (S-3298)

Phospho-VEGF Receptor 2 (Tyr1175) refers to the phosphorylated form of vascular endothelial growth factor receptor 2 (VEGFR-2) at tyrosine residue 1175, located within the kinase insert domain (KID) of the receptor, and is recognized as one of the most critical and characteristic phosphorylation sites for VEGFR-2-mediated downstream signaling. Upon stimulation by VEGF ligands (such as VEGF-A), VEGFR-2 undergoes dimerization and autophosphorylation; phosphorylation of Tyr1175 creates a highly conserved "pYXNXXV" binding motif that directly recruits and activates phospholipase Cγ (PLCγ), subsequently initiating downstream PLCγ-Ca²⁺-PKC and Ras-MAPK signaling cascades, which play central roles in regulating endothelial cell proliferation, migration, survival, and vascular permeability. Additionally, this site indirectly activates ERK1/2 via the PLCγ-PKC pathway and participates in regulating eNOS activity and nitric oxide (NO) production, thereby influencing vascular tone. Compared to other tyrosine phosphorylation sites on VEGFR-2 (such as Tyr951, Tyr1059, and Tyr1214), Tyr1175 is considered the primary hub for pro-angiogenic signaling, with its phosphorylation level directly reflecting the activation status and functional signal output of VEGFR-2. Under pathological conditions, hyperphosphorylation of Tyr1175 is closely associated with diseases such as tumor angiogenesis, age-related macular degeneration, diabetic retinopathy, and atherosclerosis, driving pathological neovascularization and promoting disease progression.