Beta-Catenin (Tyr-489)[gamma-Catenin (Tyr-480)], phospho-specific polyclonal, anti-human, mouse, rat

Background:
β-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 β-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 α- and β-Catenins. The phosphorylation of tyrosine 142 may act as a switch from the transcriptional to the adhesive role of β-Catenin. Src family kinases can also phosphorylate tyrosine 86, 489, and 654 in β-Catenin. Tyr-654 phosphorylation regulates β-Catenin binding to E-cadherin, while c-Abl phosphorylation of Tyr-489 decreases β-Catenin binding to N-Cadherin and leads to nuclear translocation and transcriptional activation.

Immunogen: Phospho-β-Catenin (Tyr-489) synthetic peptide corresponds to amino acid residues around tyrosine 489 of human β-Catenin. This peptide sequence is highly conserved in rat and mouse β-Catenin, and has high homology to the conserved site in γ-Catenin (Tyr-480).

Specificity: This antibody was cross-adsorbed to phospho-β-Catenin (Tyr-654) peptide before affinity purification using phospho-β-Catenin (Tyr-489) peptide (without carrier). The antibody detects 84 and 88kDa* proteins corresponding to the molecular mass of γ-Catenin and β-Catenin, respectively, on SDS-PAGE immunoblots of A431 cells treated with pervanadate, but does not detect these proteins in control cells.

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.