antibody

Anti-gamma-Catenin (C-terminal)

MBS470014

0.1 mL

280 USD

monoclonal

mouse

nonconjugated

western blot, ELISA, immunoprecipitation

Antibody

Anti-gamma-Catenin (C-terminal)

g-Catenin (C-terminal)

g-Catenin (C-terminal); Junction Plakoglobin; JUP; Desmoplakin III; Desmoplakin-3

Monoclonal

IgG2a

Mouse

Human, Rat, Mouse

The antibody detects an 84kDa* protein corresponding to the molecular mass of gamma-Catenin on SDS-PAGE immunoblots of A431 and Hct116 src transformed cells. In addition, this antibody recognizes only gamma-Catenin in immunoprecipitations using anti-gamma-Catenin versus anti- beta -Catenin.

Protein A Purified

Mouse monoclonal antibody purified with protein A chromatography is supplied in 100ml phosphate-buffered saline, 50% glycerol, 1 mg/ml BSA, and 0.05% sodium azide.

Store at -20 degree C. Do not aliquot. Stable for 1 year.

ELISA, Western Blot, Immunoprecipitation

ELISA: 1:2000. Immunoprecipitation: 1-5ul. Western Blot: 1:1000

Immunogen: Clone (M111) was generated from a recombinant protein that includes amino acid residues in the C-terminal region of rat gamma-Catenin. This peptide sequence is highly conserved in human and mouse gamma-Catenin.

Plakoglobin (gamma-catenin) is a catenin family member that was identified as a component of desmosomes. It associates with various cell adhesion related proteins, such as desmoglein and cadherins. gamma-Catenin has high homology to beta-catenin and, like beta-catenin, it can associate with the cadherins, E-cadherin and N-cadherin. It has been proposed that one molecule of alpha catenin and at least one molecule of beta-catenin and gamma-catenin simultaneously bind to a single cadherin molecule. A 19-amino acid sequence of desmoglein was found to be critical for binding of gamma-catenin. This region has significant homology to the catenin-binding domain of classical cadherins, thus suggesting a common mechanism for gamma-catenin localization at both adherens junctions and desmosomes. Phosphorylation of tyrosine residues in gamma-catenin can modify its interactions with other proteins. Phosphorylation of tyrosine 644 decreases gamma- catenin association with alpha-catenin, but increases binding to desmoplakin. Fer kinase can phosphorylate tyrosine 550, which increases gamma-catenin binding to alpha-catenin. Thus, tyrosinephosphorylation may be important for regulation of gamma-catenin protein-protein interactions within desmosomal complexes.

McCrea, P.D. et al. (1991) Science 254:1359. Miravet, S. et al. (2003) Mol. Cell. Biol. 23(20) :7391.

0.1 mL

280 USD