bs-70386R

DATASHEET

Host: Rabbit

Target Protein: γ-Catenin (C-terminal region)

Specificity: The antibody detects an 84kDa* protein corresponding to the molecular mass of γ-Catenin on SDS-PAGE immunoblots of A431 cells.

Clonality: Polyclonal

Isotype: IgG

Swiss Prot: P14923

Source: γ-Catenin synthetic peptide (coupled to KLH) corresponding to amino acid residues from the C-terminal region of human γ-Catenin. This peptide sequence is highly conserved in rat and mouse γ-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:

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.