VE-Cadherin (Tyr-685), Phosphospecific Antibody

Cadherins are transmembrane glycoproteins vital in calcium-dependent cell-cell adhesion during tissue differentiation. Cadherins cluster to form foci of homophilic binding units. A key determinant to the strength of the cadherin-mediated adhesion may be by the juxtamembrane region in cadherins. VE-cadherin (Cadherin 5) is the major cadherin found in endothelial cells and has important roles during angiogenesis and maintenance of barrier permeability. The cytoplasmic domain of VE-cadherin comprises the juxtamembrane domain that binds to the p120 catenin, and the carboxylterminal domain that interacts with β- or γ-catenins. Modulation of tyrosine phosphorylation on one or more of the nine tyrosine sites in the cytoplasmic domain may be important for regulating both angiogenesis and permeability. Phosphorylation of Tyr-658 and Tyr-731 alters catenin binding, restores cell migration, and decreases barrier permeability. While VEGF-induced phosphorylation of Tyr-685 occurs through c-Src, and regulates endothelial cell migration, but not permeability

Phospho-VE-Cadherin (Tyr-685) synthetic peptide (coupled to carrier protein) corresponding to amino acids surrounding tyrosine 685 in human VE-cadherin.

This antibody was cross-adsorbed to an unrelated phospho-tyrosine peptide and unphosphorylated VE-cadherin (Tyr-685) peptide before affinity purification using phospho-VE-cadherin (Tyr-685) peptide.