A phospho specific peptide corresponding to residues surrounding threonine 33 and 37 of human Beta-catenin was used as an immunogen. This antibody detects Beta-catenin phosphorylated on threonine 33 and/or 37.
Buffer
50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.
Beta-catenin is a key regulatory protein involved in cell adhesion and signal transduction through the Wnt pathway, and plays important roles in development, cellular proliferation, and differentiation (1). Beta-catenin is phosphorylated at four serine and threonine residues at the N-terminus (Ser33, Ser45, Ser37 and Thr41). Ser45 is phosphorylated by CK1, and is thought to be a priming site for the phosphorylation by glycogen synthase kinase-3 (GSK-3) (2). Wnt signaling antagonizes the action of GSK-3, which in subsequent phosphorylation steps, leads to its degradation (3). Mutations in the Beta-catenin gene, have been implicated in its accumulation and various forms of carcinomas (4).
Related Pathway
Adherens junction
Adipogenesis
Focal Adhesion
Melanogenesis
TGF Beta Signaling Pathway
Wnt Signaling Pathway
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Western blot analysis on 293T cell lysates using anti-Phospho-B-catenin (pS33/S37), 1:500 dilution. Cells were either (A) untreated (B) treated with calyculin A.
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