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Technical Data Sheet

CP2961

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β-Catenin (Tyr-489)[γ-Catenin (Tyr-480)], 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 A431 cells stimulated with pervanadate (1 mM) for 30 min (lanes 1, 3, & 5) then treated with akaline phosphatase (lanes 2, 4, & 6). The blot was probed with anti-γ-Catenin (CM1111), anti-β-Catenin (Tyr-489) conserved site (CP2961), or anti-β-Catenin (CM1181).

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Immunocytochemical labeling of β-Catenin in pervanadate-treated A431 cells. The cells were labeled with mouse monoclonal β-Catenin (CM1181) or rabbit polyclonal β-Catenin (Tyr-489) antibodies, then the antibodies were detected using appropriate secondary antibodies conjugated to Cy3.

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Application
Dilution


ELISA
1:2000


ICC
1:250


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
Beard, R.S. et al. (2011) Blood. 118(7):2007. ELISA: mouse microvascular ECs
Funakoshi S et al (2010) Am J Phys Gast Liv Phys 299(5):1054 WB: human colon cancer cells
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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 86, 489, and 654 in β-Catenin. Tyr-654 phosphorylation regulates β-Catenin binding to E-cadherin, while c-Abl phosphorylation of Tyr-489 decreases β-Catenin binding to N-Cadherin and leads to nuclear translocation and transcriptional activation.


Background References
Roura, S. et al. (1999) J Biol Chem. 274(51) :36734.
Piedra, J. et al. (2003) Mol. Cell. Biol. 23(7):2287.
Brembeck, F.H. et al. (2004) Genes Dev. 18(18):2225.
Rhee, J. et al. (2007) Nat. Cell Biol. 9(8):883.
Immunogen
Phospho-β-Catenin (Tyr-489) synthetic peptide corresponds to amino acid residues around tyrosine 489 of human β-Catenin. This peptide sequence is highly conserved in rat and mouse β-Catenin, and has high homology to the conserved site in γ-Catenin (Tyr-480).
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-β-Catenin (Tyr-654) peptide before affinity purification using phospho-β-Catenin (Tyr-489) peptide (without carrier). The antibody detects 84 and 88kDa* proteins corresponding to the molecular mass of γ-Catenin and β-Catenin, respectively, on SDS-PAGE immunoblots of A431 cells treated with pervanadate, but does not detect these proteins in control 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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