Alpha1-Catenin (Tyr-148), phospho-specific polyclonal, anti-human, mouse, rat, chicken

Background:
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.

Immunogen: Phospho-α1-Catenin (Tyr-148) synthetic peptide (coupled to KLH) corresponding to amino acid residues around tyrosine 148 in human α1-Catenin. This peptide sequence is highly conserved in rat and mouse α1-Catenin, but is not conserved in α2-Catenin or α3-Catenin.

Specificity: This antibody was cross-adsorbed to unrelated phospho-tyrosine peptide before affinity purification using phospho-α1-Catenin (Tyr-148) peptide (without carrier). The antibody detects a 102 kDa* protein corresponding to the molecular mass of α1-Catenin on SDS-PAGE immunoblots of rat PC12 cells treated with pervanadate.

Buffer/Storage:
Rabbit polyclonal, affinity-purified antibody is supplied in 100µl phosphate-buffered saline, 50% glycerol, 1 mg/ml BSA, and 0.05% sodium azide. Store at –20°C. Stable for 1 year.