bs-70370R

DATASHEET

Host: Rabbit

Target Protein: VE-Cadherin (C-terminal)

Specificity: 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.

Clonality: Polyclonal

Isotype: IgG

Swiss Prot: P33151

Source: VE-Cadherin synthetic peptide (coupled to carrier protein) corresponds to amino acids from the C-terminal region of human VE-cadherin.

Purification: Antigen Affinity purification

Storage Buffer: PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol

Storage: Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C.

Background:

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