|Detection of Human E‑Cadherin by Western Blot. Western blot shows lysates of MCF‑7 human breast cancer cell line, BT‑20 human breast cancer cell line, and T47D human breast cancer cell line. PVDF membrane was probed with 2 µg/mL of Mouse Anti-Human E‑Cadherin Monoclonal Antibody (Catalog # MAB18382) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF018). A specific band was detected for E‑Cadherin at approximately 120 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
Epithelial (E) - Cadherin (ECAD), also known as cell-CAM120/80 in the human, uvomorulin in the mouse, Arc-1 in the dog, andL-CAM in the chicken, is a member of the Cadherin family of cell adhesion molecules. Cadherins are calcium-dependent transmembrane proteins which bind to one another in a homophilic manner. On their cytoplasmic side, they associate with the three catenins, alpha, beta, and gamma (plakoglobin). This association links the cadherin protein to the cytoskeleton. Without association with the catenins, the cadherins are non-adhesive. Cadherins play a role in development, specifically in tissue formation. They may also help to maintain tissue architecture in the adult. E-Cadherin may also play a role in tumor development, as loss of E-Cadherin has been associated with tumor invasiveness. E-Cadherin is a classical cadherin molecule. Classical cadherins consist of a large extracellular domain which contains DXD and DXNDN repeats responsible for mediating
calcium-dependent adhesion, a single-pass transmembrane domain, and a short carboxy-terminal cytoplasmic domain responsible for interacting with the catenins. E-Cadherin contains five extracellular calcium-binding domains of approximately 110 amino acids each.
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