| Product Name | Catenin-_ E/N Polyclonal Antibody |
|---|---|
| Description | Associates with the cytoplasmic domain of a variety of cadherins. The association of catenins to cadherins produces a complex which is linked to the actin filament network, and which seems to be of primary importance for cadherins cell-adhesion properties. Can associate with both E- and N-cadherins. Originally believed to be a stable component of E-cadherin/catenin adhesion complexes and to mediate the linkage of cadherins to the actin cytoskeleton at adherens junctions. In contrast, cortical actin was found to be much more dynamic than E-cadherin/catenin complexes and CTNNA1 was shown not to bind to F-actin when assembled in the complex suggesting a different linkage between actin and adherens junctions components. The homodimeric form may regulate actin filament assembly and inhibit actin branching by competing with the Arp2/3 complex for binding to actin filaments. May play a crucial role in cell differentiation. |
| Synonyms | CTNNA1, Catenin alpha-1, Alpha E-catenin, Cadherin-associated protein, Renal carcinoma antigen NY-REN-13, CTNNA2, CAPR, Catenin alpha-2, Alpha N-catenin, Alpha-catenin-related protein |
| Host | Rabbit |
| Immunogen | Synthesized peptide derived from the C-terminal region of human Catenin-_ E/N |
| Isotype | IgG |
| Reactivity | Human, Mouse, Rat |
| Applications | ELISA, IF, IHC, WB |
| Form | PBS with 0.02% sodium azide, 0.5% BSA and 50% glycerol, pH7.4 |
| Uniprot | P35221/P26232 |
| Background | Associates with the cytoplasmic domain of a variety of cadherins. The association of catenins to cadherins produces a complex which is linked to the actin filament network, and which seems to be of primary importance for cadherins cell-adhesion properties. Can associate with both E- and N-cadherins. Originally believed to be a stable component of E-cadherin/catenin adhesion complexes and to mediate the linkage of cadherins to the actin cytoskeleton at adherens junctions. In contrast, cortical actin was found to be much more dynamic than E-cadherin/catenin complexes and CTNNA1 was shown not to bind to F-actin when assembled in the complex suggesting a different linkage between actin and adherens junctions components. The homodimeric form may regulate actin filament assembly and inhibit actin branching by competing with the Arp2/3 complex for binding to actin filaments. May play a crucial role in cell differentiation. |
| Supplier | Elabscience |
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