|Detection of E‑Cadherin in D3 Mouse Cell Line by Flow Cytometry. D3 mouse embryonic stem cell line was stained with Rat Anti-Mouse E‑Cadherin PE‑conjugated Monoclonal Antibody (Catalog # FAB7481P, filled histogram) or isotype control antibody (Catalog # IC006P, open histogram). Cells were stained in a buffer containing Ca2+ and Mg2+. View our protocol for Staining Membrane-associated Proteins.|
Epithelial (E) - Cadherin (ECAD), also known as cell-CAM120/80 in the human, uvomorulin in the mouse, Arc-1 in the dog, and L-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. A soluble form of E-Cadherin can be released from epithelial cell surfaces by proteolysis. E‑Cadherin contains five extracellular calcium‑binding domains of approximately 110 amino acids each.
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