VE-Cadherin (C-terminal) 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

The antibody detects a 140 kDa* band corresponding to VE-cadherin in western blots of human endothelial cells, and this reactivity can be specifically blocked using VE-cadherin peptide (CX2235) . This sequence has significant homology to the conserved site in rat and mouse, and has less than 50% homology with other cadherins.