| Overview |
| bs-70377r-100ul |
| α1-Catenin (N-terminal region) Antibody |
| WB |
| The antibody detects a 102 kDa* protein corresponding to the molecular mass of α1-Catenin on SDS-PAGE immunoblots of rat PC12 and mouse SYF cells. This peptide sequence is highly conserved in rat and mouse α1-Catenin, and has some homology to α2-Catenin or α3-Catenin. |
| Human, Mouse, Rat, Chicken |
| Specifications |
| Unconjugated |
| Rabbit |
| α1-Catenin synthetic peptide (coupled to KLH) corresponding to amino acid residues from the N-terminal region of human α1-Catenin. |
| Polyclonal |
| IgG |
| Antigen Affinity purification |
| PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol |
| Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C. |
| Target |
| P35221 |
| alphaE-catenin, catenin alpha1, catenin |
| α-catenins are cadherin interacting proteins with homology to vinculin. Three α-catenin genes have been described including α1-catenin (αE-Catenin), α2-catenin (αN-catenin), and α3-catenin (αT-catenin). α1-catenin has 81% homology with α2-catenin and 60% homology with α3-catenin. These α-catenin isoforms may have similar roles since each binds cadherins. However, their expression patterns are both overlapping and distinct. α1-catenin was identified in epithelial cells, and is expressed in various cell types. α2-catenin is enriched in the nervous system, and α3-catenin is expressed highest in testis and heart. Phosphorylation may regulate the activity of α1-catenin, since tyrosine phosphorylation of Tyr-148 occurs during intercellular adhesion. This site is dephosphorylated by SHP2, which inhibits α1-catenin binding to β-catenin and translocation to the plasma membrane. Phosphorylation of α1-catenin at Tyr-148 may be important for inhibition of cell transformation, and dephosphorylation of this site may be important during SHP2-mediated cell transformation. |
| Application Dilution |
| WB |
1:300-5000 |
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