Western blot analysis of whole cell lysates from NIH/3T3 cells treated with calyculin A, using Phospho-beta-Catenin (Ser33/37/Thr41) Antibody #9561 alone (left) and the same antibody preincubated with Phospho-beta-Catenin (Ser33/37/Thr41) Blocking Peptide (right).
For Western immunoblotting, add 10 µl of antibody and 10 µl of blocking peptide to 10 ml of antibody dilution buffer, and incubate at room temperature for 2 hours before allowing to react with the blot.
Supplied in 20 mM potassium phosphate (pH 7.0), 50 mM NaCl, 0.1 mM EDTA, 1 mg/ml BSA and 5% glycerol. Store at –20°C.
This peptide is used to block Phospho-beta-Catenin (Ser33/37/Thr41) Antibody # 9561 reactivity.
The quality of the peptide was evaluated by reversed-phase HPLC and by mass spectrometry. The peptide blocks Phospho-beta-Catenin (Ser33/37/Thr41) Antibody #9561 signal completely in Western blotting.
β-Catenin is a key downstream effector in the Wnt signaling pathway (1). It is implicated in two major biological processes in vertebrates: early embryonic development (2) and tumorigenesis (3). CK1 phosphorylates β-catenin at Ser45. This phosphorylation event primes β-catenin for subsequent phosphorylation by GSK-3β (4-6). GSK-3β destabilizes β-catenin by phosphorylating it at Ser33, Ser37, and Thr41 (7). Mutations at these sites result in the stabilization of β-catenin protein levels and have been found in many tumor cell lines (8).
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