|Detection of E‑Cadherin in MCF‑7 Human Cell Line by Flow Cytometry. MCF‑7 human breast cancer cell line was stained with Goat Anti-Human E‑Cadherin Alexa Fluor® 647‑conjugated Antigen Affinity-purified Polyclonal Antibody (Catalog # FAB748R, filled histogram) or isotype control antibody (Catalog # IC108R, open histogram). 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. E‑Cadherin contains five extracellular calcium‑binding domains of approximately 110 amino acids each.
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