Catenin Alpha 1 (CTNNA1) Peptide
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Description
Catenin Alpha 1 (CTNNA1) Peptide is a synthetic peptide.
Documents del producto
Product specifications
| Category | Proteins and Peptides |
| Immunogen Target | Catenin Alpha 1 (CTNNA1) |
| Host | Synthetic |
| Recommended Dilution | BL (predicted): 0.5 mg/ml. Optimal dilutions/concentrations should be determined by the end user. |
| Conjugation | Unconjugated |
| Observed MW | Sequence Fragment: Internal region: C-KREKQDETQTKIK |
| Size 1 | 100 µg |
| Form | Lyophilized Reconstitute in deionized water. |
| Tested Applications | P-ELISA |
| Buffer | Prior to lyophilization: Deionized water. |
| Availability | Shipped within 5-10 working days. |
| Storage | Aliquot and store at -20°C. Avoid repeated freeze/thaw cycles. |
| Dry Ice | No |
| Gene ID | 1495, 12385, 307505 |
| NCBI Accession | NP_001894.2 |
| Background | Protein CTNNA1 |
| Note | This product is for research use only. Not for human consumption, cosmetic, therapeutic or diagnostic use. |
Descripción
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This gene encodes a member of the catenin family of proteins that play an important role in cell adhesion process by connecting cadherins located on the plasma membrane to the actin filaments inside the cell. The encoded mechanosensing protein contains three vinculin homology domains and undergoes conformational changes in response to cytoskeletal tension, resulting in the reconfiguration of cadherin-actin filament connections. Certain mutations in this gene cause butterfly-shaped pigment dystrophy.
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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.
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