repeats of approximately 100 residues in their extracellular domain. Cadherins mediate calcium-dependent cell-cell adhesion and play critical roles in normal tissue development . The classic cadherin subfamily includes N-, P-, R-, B-, and E-cadherins, as well as about ten other members that are found in adherens junctions, a cellular structure near the apical surface of polarized epithelial cells. The cytoplasmic domain of classical cadherins interacts with beta-catenin, gamma-catenin (also called plakoglobin), and p120 catenin. beta-catenin and gamma-catenin associate with alpha-catenin, which links the cadherin-catenin complex to the actin cytoskeleton . While beta- and gamma-catenin play structural roles in the junctional complex, p120 regulates cadherin adhesive activity and trafficking . Investigators consider E-cadherin an active suppressor of invasion and growth of many epithelial cancers (1-3). Research studies indicate that cancer cells have upregulated N-cadherin in addition to loss of E-cadherin. This change in cadherin expression is called the cadherin switch. N-cadherin cooperates with the FGF receptor, leading to overexpression of MMP-9 and cellular invasion . Research studies have shown that in endothelial cells, VE-cadherin signaling, expression, and localization correlate with vascular permeability and tumor angiogenesis . Investigators have also demonstrated that expression of P-cadherin, which is normally present in epithelial cells, is also altered in ovarian and other human cancers .
The antibody was affinity-purified from mouse antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Formulierung:
Mouse IgG1. Liquid in PBS containing 50% glycerol, 0.2% BSA and 0.01% sodium azide.
