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 (1). 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 B-catenin, Y-catenin (also called plakoglobin), and p120 catenin. B-catenin and Y-catenin associate with A-catenin, which links the cadherin-catenin complex to the actin cytoskeleton (1,2). Unlike B- and Y-catenin, p120 regulates cadherin adhesive activity and trafficking rather than having a structural role in the junctional complex (1-4). E-cadherin is considered an active suppressor of invasion and growth of many epithelial cancers (1-3). Recent studies indicate that cancer cells have up-regulated 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 over-expression of MMP-9 and cellular invasion (3). In endothelial cells, VE-cadherin signaling, expression, and localization correlate with vascular permeability and tumor angiogenesis (5,6). Expression of P-cadherin, which is normally present in epithelial cells, is also altered in ovarian and other human cancers (7,8).
Applications:
Suitable for use in Western Blot and Immunoprecipitation. Other applications not tested.
Recommended Dilution:
Western Blot: 1:1000
Immunoprecipitation: 1:200
Optimal dilutions to be determined by the researcher.
Storage and Stability:
May be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Aliquots are stable for at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.