Anti-E-Cadherin Antibody
serum, Upstate®
Cadherin-1 (UniProt: P12830; also known as CAM 120/80, Epithelial cadherin, E-cadherin, Uvomorulin, CD324) is encoded by the CDH1 (also known as CDHE, UVO) gene (Gene ID: 999) in human. Cadherins are calcium-dependent cell adhesion molecules that participate in cell-cell adhesion during embryogenesis, development, organogenesis, and differentiation. E-cadherin is a single-pass type I membrane glycoprotein that is mainly expressed in non-neural epithelial tissues. It is synthesized with a signal peptide (aa 1-22) and a propeptide (aa 23-154) that are subsequently cleaved off to produce the mature form that contains an extracellular domain (aa 155-709), a transmembrane domain (aa 710-730), and a cytoplasmic domain (aa 731-882). N-glycosylation at Asn-637 is shown to be essential for its expression, folding, and trafficking. E-cadherin is known to contain five cadherin domains. Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain. Post-translationally it can be cleaved into three chains: E-Cad/CTF1 (aa 701-882); E-Cad/CTF2 (aa 732-882); and E-Cad/CTF3 (aa 751-882). During apoptosis or with calcium influx, it is cleaved by a membrane-bound metalloproteinase (ADAM10; at residues 700-701), which causes disruption of cell-cell adhesion and the subsequent release of b-catenin into the cytoplasm. The residual membrane-tethered cleavage product is then rapidly degraded via an intracellular proteolytic pathway. It can also be cleaved by PS1/g-secretase (at residues 731-732) and this cleavage promotes disassembly of adherens junctions. Caspase 3 can cleave it at residues 750-751, which releases the cytoplasmic tail resulting in disintegration of the actin microfilament system. (Ref.: Marambaud, M., et al. (2002). EMBO J. 21(8); 1948-1956; Steinhausen, U., et al. (2001). J. Biol. Chem. 276(7); 4972-4980; Ito, K., et al. (1999). Oncogene. 18(50); 7080-7090).
