Cadherins comprise a family of Ca-dependent adhesion molecules that function to mediate cell-cell binding critical to the maintenance of tissue structure and morphogenesis. Cadherins consist of large extracellular domains characterized by a series of five homologous NH2 terminal repeats. The most distal of cadherins is thought to be responsible for binding specificity, transmembrane domains and carboxy terminal domains. The relative short intracellular domains interact with a variety of cytoplasmic proteins, such as β-catenin, to regulate cadherin function.

E-cadherin is an intercellular adhesion molecule present in epithelial cells. Anti-E-cadherin stains glandular epithelium, as well as lung, gastrointestinal and ovarian adenocarcinomas. A decreased expression of E-cadherin is associated with metastatic potential and poor prognosis in breast cancer and esophagus cancer. A panel of antibodies against E-cadherin and p120 is also used to differentiate ductal (membranous staining) and lobular breast cancer (cytoplasmic staining). Anti-E-cadherin also stains some thyroid cancers.