Anti-E-Cadherin / CDH1, clone rCDH1/1525

1 mg/ml in 1X PBS, BSA free, sodium azide free. Recognizes a protein of 80-120kDa, identified as E-cadherin. Cadherins comprise a family of Ca2+-dependent adhesion molecules that function to mediate cell-cell binding critical to the maintenance of tissue structure and morphogenesis. The classical cadherins, E-, N- and P-cadherin, consist of large extracellular domains characterized by a series of five homologous NH2 terminal repeats. The relatively short intracellular domains interact with a variety of cytoplasmic proteins, such as b-catenin, to regulate cadherin function. E-cadherin plays an important role in epithelial cell adhesion. A decreased expression of E-cadherin is associated with metastatic potential and poor prognosis in breast cancer, prostate and esophageal cancer. In combination with p120 Catenin, it is useful for the differentiation between ductal (E-cadherin +) and lobular (E-cadherin -) breast carcinomas. It may also help in diagnosis of mesothelioma. Protein function: Cadherins are calcium-dependent cell adhesion proteins (PubMed:11976333). They preferentially interact with themselves in a homophilic manner in connecting cells, cadherins may thus contribute to the sorting of heterogeneous cell types. CDH1 is involved in mechanisms regulating cell-cell adhesions, mobility and proliferation of epithelial cells (PubMed:11976333). Promotes organization of radial actin fiber structure and cellular response to contractile forces, via its interaction with AMOTL2 which facilitates anchoring of radial actin fibers to CDH1 junction complexes at the cell membrane. Has a potent invasive suppressor role. It is a ligand for integrin alpha-E/beta-7. [The UniProt Consortium]