| Applications | ICC/IF |
| Clonality | Polyclonal |
| Host | Goat |
| Conjugate | NL493 |
| Specificity | Detects human E-Cadherin in direct ELISAs and Western blots. In direct ELISAs and Western blots, approximately 15% cross-reactivity with recombinant mouse E-Cadherin is observed. |
| Isotype | IgG |
| Clonality | Polyclonal |
| Host | Goat |
| Gene | CDH1 |
| Innovator's Reward | Test in a species/application not listed above to receive a full credit towards a future purchase. |
| Storage | Store the unopened product at 2 - 8° C. Do not use past expiration date. Protect from light. |
| Buffer | Supplied in a saline solution containing BSA and Sodium Azide. |
| Preservative | Sodium Azide |
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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