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Technical Data Sheet

CP1081

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β-Catenin (Tyr-142)[γ-Catenin (Tyr-133)], phospho-specific
Rabbit Polyclonal
Price
Size
Species Reactivity
MW

$295
100 μl
Hu, Rt, Ms
92 kDa

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Western blot analysis of Hct116 src transformed cells (20 µg/lane) serum starved overnight or treated with pervanadate (1 mM) for 30 min. The blot was probed with anti-β-Catenin or anti-β-Catenin (Tyr-142).

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Immunocytochemical labeling of phosphorylated β-Catenin in paraformaldehyde-fixed and NP-40-permeabilized rabbit spleen fibroblasts. The cells were labeled with mouse monoclonal β-Catenin and rabbit polyclonal β-Catenin (Tyr-142) antibodies, then the antibodies were detected using appropriate secondary antibodies conjugated to Cy3.

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Application
Dilution


ELISA
1:2000


ICC
1:100


WB
1:500



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
Tsuneki, M. et al. (2014) Mol Cell Biol. 34(24): 4485 IF: mouse EOMA, brain endothelial cells
Qi, F. et al. (2013) Am J Pathol. 183(5):1654. WB: human mesothelial
Krejci, P. et al. (2012) PLoS ONE. 7(4):e35826. WB: rat chondrosarcoma cells
Beard, R.S. et al. (2011) Blood. 118(7):2007. ELISA: mouse microvascular ECs
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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 654 in the C-terminal armadillo repeat of β-Catenin. This phosphorylation regulates β-Catenin binding to E-cadherin. Thus, site-specific tyrosine phosphorylation of β-Catenin may regulate specific protein-protein interactions leading to changes in cell adhesion.


Background References
Ozawa, M. et al. (1990) Proc. Natl. Acad. Sci. USA 87:4246.
Piedra, J. et al. (2003) Mol. Cell. Biol. 23(7):2287.
Brembeck, F.H. et al. (2004) Genes Dev. 18(18):2225.
Immunogen
Phospho-β-Catenin (Tyr-142) synthetic peptide (coupled to KLH) corresponding to amino acid residues around tyrosine 142 of human β-Catenin. This peptide sequence has one amino acid difference from a sequence around tyrosine 133 of human γ-Catenin. These human sequences are highly conserved in rat and mouse β- and γ-Catenins.
Buffer and 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.
Specificity
This antibody was cross-adsorbed to phospho-tyrosine coupled to agarose before affinity purification using phospho-β-Catenin (Tyr-142) peptide (without carrier). The antibody detects a 92kDa* protein corresponding to the molecular mass of β-Catenin on SDS-PAGE immunoblots of Hct116 src-transformed cells treated with pervanadate, but not in control cells. Similar results were observed in pervanadate-treated A431 and human endothelial cells.

*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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