Invitrogen™ Phospho-beta Catenin/gamma Catenin (Tyr654, Tyr644) Polyclonal Antibody

Description

This antibody was cross-adsorbed to phospho-beta-Catenin (Tyr-86) peptide before affinity purification using phospho-beta-Catenin (Tyr-654) peptide (without carrier). The antibody detects 84 and 88kDa* proteins corresponding to the molecular mass of gamma-Catenin and beta-Catenin, respectively, on SDS-PAGE immunoblots of A431 cells treated with pervanadate, but does not detect these proteins in control cells.

beta-Catenin is a 92 kDa protein that binds to the cytoplasmic tail of E-Cadherin. The cadherins, transmembrane adhesion molecules, are found with catenins at adherens junctions. Deletions in the cytoplasmic domain of E-Cadherin eliminate catenin binding and result in a loss of cell adhesion. Tyrosine phosphorylation of beta-Catenin can regulate its interaction with critical components of adherens junctions. Both Fer and Fyn kinases phosphorylate tyrosine 142 in vitro. Overexpression of these kinases in epithelial cells disrupts interactions between alpha- and beta-Catenins. The phosphorylation of tyrosine 142 may act as a switch from the transcriptional to the adhesive role of beta-Catenin. Src family kinases can also phosphorylate tyrosine 86 and 654 in beta-Catenin. The Tyr-654 phosphorylation regulates beta-Catenin binding to E-cadherin. Thus, site-specific tyrosine phosphorylation of beta-Catenin may regulate protein-protein interactions leading to changes in cell adhesion.