Cell Signaling Technology

Product Pathways - Adhesion

Acetyl-β-Catenin (Lys49) Antibody #9534

Applications Reactivity MW (kDa) Source
W H (M) (R) (Pg) 92 Rabbit

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human  M=Mouse  R=Rat  Pg=Pig
Species enclosed in parentheses are predicted to react based on 100% sequence homology. Species cross-reactivity is determined by Western blot.

Specificity / Sensitivity

Acetyl-β-Catenin (Lys49) Antibody detects endogenous β-catenin only when acetylated at Lys49.

Source / Purification

Polyclonal antibodies are produced by immunizing rabbits with a synthetic acetylated peptide (KLH-coupled) corresponding to residues surrounding Lys49 of human β-catenin. Antibodies were purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of total cell lysates from 293 cells, untransfected or transiently transfected with a construct expressing CBP, using Acetyl-β-Catenin (Lys49) Antibody (Top), or total β-Catenin Antibody (Amino-terminal Antigen) #9581 (Bottom).

Background

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 on Ser45. This phosphorylation event primes β-catenin for subsequent phosphorylation by GSK-3 (4-6). GSK-3β destabilizes β-catenin by phosphorylating it at Ser33, Ser37 and Thr41 (7). Mutations in these phosphorylation sites, which result in the stabilization of β-catenin protein levels, have been found in many tumor cell lines (8).

Lys49 lies in a region that contains several Ser/Thr residues whose phosphorylation status regulates the stability of β-catenin and is one of few residues frequently mutated in thyroid anaplastic carcinoma (9). CBP (CREB-binding protein) binds and acetylates β-catenin at Lys49 (10, 11).

  1. Cadigan, K.M. and Nusse, R. (1997) Genes Dev. 11, 3286-3305.
  2. Wodarz, A. and Nusse, R. (1998) Annu. Rev. Cell. Dev. Biol. 14, 59-88.
  3. Polakis, P. (1999) Curr. Opin. Genet. Dev. 9, 15-21.
  4. Amit, S. et al. (2002) Genes Dev. 16, 1066-1076.
  5. Lin, C. et al. (2002) Cell 108, 837-847.
  6. Yanagawa, S. et al. (2002) EMBO J. 21, 1733-1742.
  7. Yost, C. et al. (1996) Genes Dev. 10, 1443-1454.
  8. Morin, P.J. (1997) Science 275, 1787-1790.
  9. Polakis, P. (2000) Genes Dev. 14, 1837-5181.
  10. Takemaru, K.I. and Moon, R.T. (2000) J. Cell Biol. 149, 249-254.
  11. Wolf, D. et al. (2002) J. Biol. Chem. 277, 25562-25567.

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