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Technical Data Sheet

CM1111

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γ-Catenin (C-terminal)
Mouse Monoclonal IgG2a
Price
Size
Species Reactivity
MW

$245
100 μl
Hu, Rt, Ms
84 kDa

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Western blot analysis of anti-γ-Catenin (C-terminal) immunoprecipitates from pervanadate-treated A431. The immunoprecipitates were untreated (lanes 1,3,7) or treated with alkaline phosphatase (lanes 2,4,8). The blots were probed with γ-Catenin (a.a. 545-555), γ-Catenin (Tyr-550) or γ-Catenin (C-terminal) antibodies. The anti-γ-Catenin (Tyr-550) was used in the presence of γ-Catenin (Tyr-550) (lane 5) or γ-Catenin (Tyr-644) (lane 6) peptides.

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Immunocytochemical labeling of phosphorylated γ-Catenin in control (Top) and pervanadate-treated (Bottom) A431 cells. The cells were co-labeled with mouse monoclonal γ-Catenin (CM1111) or rabbit polyclonal γ-Catenin (Tyr-550) antibodies, then the antibodies were detected using appropriate secondary antibodies conjugated to Cy2 or Cy3.

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Application
Dilution


ELISA
1:2000


ICC
1:50


IP
1:100


WB
1:1000



End user should determine optimal dilution for their particular applications and experiments.Western blot membranes were incubated with diluted antibody in 5% non-fat milk, PBS, 0.04% Tween20 for 1hour at room temperature.
Product References
Cooksley-Decasper, S. et al. (2012) PLoS One 7(10):e47985. WB: human macrophages
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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.


Background References
McCrea, P.D. et al. (1991) Science 254:1359.
Miravet, S. et al. (2003) Mol. Cell. Biol. 23(20) :7391.
Immunogen
Clone (M111) was generated from a recombinant protein that includes amino acid residues in the C-terminal region of rat γ-Catenin. This peptide sequence is highly conserved in human and mouse γ-Catenin.
Buffer and Storage
Mouse monoclonal antibody purified with protein A chromatography 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.
Specificity
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. In addition, this antibody recognizes only γ-Catenin in immunoprecipitations using anti-γ-Catenin versus anti-β-Catenin.

*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
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