Anti-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

Our VE-Cadherin (Tyr-685) rabbit polyclonal phosphospecific primary antibody from PhosphoSolutions is produced in-house. It detects human, mouse, and rat VE-Cadherin (Tyr-685) and is antigen affinity purified. It is great for use in WB.

Phospho-VE-Cadherin (Tyr-685) synthetic peptide (coupled to carrier protein) corresponding to amino acids surrounding tyrosine 685 in human VE-cadherin. This sequence has significant homology to the conserved site in rat and mouse VE-cadherin, but is not conserved in other cadherins.

For research use only. Not intended for therapeutic or diagnostic use. Use of all products is subject to our terms and conditions, which can be viewed on our website.

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. The purified antibody detects a 140 kDa* band corresponding to VE-cadherin in western blots of human endothelial cells treated with pervanadate, and this band is not detected in untreated cells or after alkaline phosphatase treatment.