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Alpha-1 Catenin AntibodyRabbit Monoclonal Antibody
| Country | United States
Ordering Information
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| Catalog # | Size | Availability | Price | |
| AJ1026a | 100ul 400 ul | 2-3 days | $ 315.00 | DISCONTINED INQUIRE CLICK INQUIRE Add to cart |
- Specification
- Citiations : 0
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- Backgrounds
Alpha-1 Catenin Antibody - Product info | |
| Application | WB, IHC
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| Primary Accession | P35221 |
| Reactivity | Human, Mouse, Rat |
| Clone Names | EP1793Y |
| Calculated MW | 100071 Da |
| Gene ID 1495 | |
| Other Names CTNNA1, Catenin alpha-1, Cadherin-associated protein;Alpha E-catenin;NY-REN-13 antigen | |
| Target/Specificity A synthetic peptide corresponding to residues near the N-terminus of human α-1 catenin was used as an immunogen. | |
| Dilution WB~~1:1000~10000 IHC~~1:100~250 | |
| Format 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA. | |
| Storage Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. | |
| Precautions Alpha-1 Catenin Antibody is for research use only and not for use in diagnostic or therapeutic procedures. | |
Alpha-1 Catenin Antibody - Protein Information | |
| Name CTNNA1 | |
| Function 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 | |
| Cellular Location Cytoplasm, cytoskeleton. Cell junction, adherens junction. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junction. Note=Found at cell-cell boundaries and probably at cell-matrix boundaries | |
| Tissue Location Expressed ubiquitously in normal tissues. | |
Alpha-1 Catenin Antibody - Related products
AP6582a: CTNA1 Antibody (N-term)
AP6582b: CTNA1 Antibody (C-term)
RI11304: CTNNA1 predesign siRNA
LY10949a: CTNNA1 Over-expression Lysate
BP6582a: CTNA1 Antibody (N-term) Blocking Peptide
BP6582b: CTNA1 Antibody (C-term) Blocking Peptide
Alpha-1 Catenin Antibody - Application data
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A. Western blot analysis on HeLa cell lysate using anti-Alpha-1 Catenin RabMAb (Cat. #AJ1026a), dilution 1:50,000.
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B. Immunohistochemical staining of paraffin-embedded human breast carcinoma using anti-Alpha-1 Catenin RabMAb (Cat. #AJ1026a).
Alpha-1 Catenin Antibody - Research Areas
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BACKGROUND
Cadherin and catenin compose cell adhesion complex and are indispensable for tight cell-cell adhesion. Dysfunction of this adhesion complex causes dissociation of cancer cells from primary tumor nodules, thus possibly contributing to cancer invasion and metastasis (1). At least three proteins (alpha, beta, and gamma catenin) comprise the cytoplasmic domain of the cadherin cell-cell adhesion complex. Data, with the reported structure of other catenin genes, suggest that vinculin and alpha-catenin generate a superfamily of proteins mediating membrane-cytoskeletal associations (2). Presenilin-1 (PS1) overexpression in human kidney cells enhances cell-cell adhesion and data show that PS1 incorporates into the cadherin/catenin adhesion system and regulates cell-cell adhesion. PS1 concentrates at intercellular contacts in epithelial tissue; in brain, it forms complexes with both E- and N-cadherin and concentrates at synaptic adhesions (3).
REFERENCES
1. Oda T, et al. Biochem Biophys 193(3):897-904, 1993
2. Rimm DL, et al. Biochem Biophys 203(3):1691-9, 1994
3. Georgakopoulos A, et al. Mol Cell 4(6):893-902, 1999
