Rabbit Polyclonal antibody to CD325

Cadherins are a superfamily of transmembrane glycoproteins that contain cadherin 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 β~catenin, γ~catenin (also called plakoglobin), and p120 catenin. β~catenin and γ~catenin associate with α~catenin, which links the cadherin~catenin complex to the actin cytoskeleton. While β~ and γ~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. 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.