Gamma-Catenin (Tyr-550), phospho-specific polyclonal, anti-human, mouse, rat

Background:
Plakoglobin (γ-Catenin) is a catenin family member identified as a component of desmosomes. γ-Catenin has high homology to β-catenin and, like β-catenin, it can associate with the cadherins, E-cadherin and N-cadherin. One molecule of α-catenin and at least one molecule of β-catenin and γ-Catenin simultaneously bind to a single cadherin molecule. A 19-amino acid sequence of desmoglein was found to be critical for binding of γ-Catenin. Similar catenin-binding domains found in cadherins, suggest a common mechanism for γ-Catenin localization to both adherens junctions and desmosomes. Phosphorylation of tyrosine residues in γ-Catenin can modify its interactions with other proteins. Phosphorylation of tyrosine 644 decreases γ-Catenin association with α-catenin, but increases binding to desmoplakin. Fer kinase can phosphorylate tyrosine 550, which increases γ-Catenin binding to α-catenin. Thus, tyrosine phosphorylation may be important for regulation of γ-Catenin protein-protein interactions within desmosomal complexes.

Immunogen: Phospho-γ-Catenin (Tyr-550) synthetic peptide (coupled to KLH) corresponding to amino acid residues around tyrosine 550 of human γ-Catenin. This peptide sequence is highly conserved in rat and mouse γ-Catenin.

Specificity: This antibody was cross-adsorbed to both phospho-tyrosine coupled to agarose and to dephosphorylated γ-Catenin (Tyr-550) peptide before affinity purification using phospho-γ-Catenin (Tyr-550) peptide (without carrier). The antibody detects an 84kDa* protein corresponding to the molecular mass of γ-Catenin on SDS-PAGE immunoblots of A431 and Hct116 src transformed cells treated with pervanadate (1 mM for 30 min), but not 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.