Anti-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

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

VE-Cadherin synthetic peptide (coupled to carrier protein) corresponds to amino acids from the C-terminal region of human VE-cadherin. This sequence has significant homology to the conserved site in rat and mouse, and has less than 50% homology with 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.

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) .