Phospho-VEGF Receptor 2 (Tyr1059) Recombinant Rabbit mAb (S-3425)

Phospho-VEGF Receptor 2 (Tyr1059) refers to the phosphorylated form of vascular endothelial growth factor receptor 2 (VEGFR-2, also known as KDR or Flk-1) at tyrosine residue 1059, which is located within the kinase insert domain of the receptor and serves as a key docking site for regulating downstream signaling pathways following receptor activation. Upon binding of VEGF ligands (such as VEGF-A) to VEGFR-2, the receptor dimerizes and initiates an autophosphorylation cascade; phosphorylation of Tyr1059 creates a high-affinity binding site that specifically recruits and activates the adaptor protein SHB (Src homology 2 domain-containing adapter protein B), which in turn mediates the activation of downstream PI3K-Akt and MAPK signaling pathways, playing a central role in regulating endothelial cell survival, proliferation, and migration. Unlike the dual phosphorylation site Tyr1054/1059, which is more directly involved in regulating kinase activity, phosphorylation of Tyr1059 alone is more focused on signaling complex assembly and is also associated with cell adhesion, vascular permeability regulation, and nitric oxide (NO) production. Under pathological conditions, aberrant phosphorylation of Tyr1059 is observed in diseases such as tumor angiogenesis, diabetic retinopathy, and rheumatoid arthritis, where it promotes pathological neovascularization through sustained activation of downstream survival signals.