bs-70378R

DATASHEET

Host: Rabbit

Target Protein: α1-Catenin (Tyr-148)

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. This peptide sequence is highly conserved in rat and mouse α1-Catenin, but is not conserved in α2-Catenin or α3-Catenin.

Modification Site: Tyr-148

Clonality: Polyclonal

Isotype: IgG

Swiss Prot: P35221

Source: Phospho-α1-Catenin (Tyr-148) synthetic peptide (coupled to KLH) corresponding to amino acid residues around tyrosine 148 in human α1-Catenin.

Purification: Antigen Affinity purification

Storage Buffer: PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol

Storage: 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.

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.