Cell Signaling Technology

Product Pathways - Wnt / Hedgehog / Notch

β-Catenin Antibody (Amino-terminal Antigen) #9581

Applications Reactivity MW (kDa) Source
W IP IF-F F H M R Mk Hm B 92 kDa Rabbit

Applications Key:  W=Western Blotting  IP=Immunoprecipitation  IF-F=Immunofluorescence (Frozen)  F=Flow Cytometry
Reactivity Key:  H=Human  M=Mouse  R=Rat  Mk=Monkey  Hm=Hamster  B=Bovine
Species enclosed in parentheses are predicted to react based on 100% sequence homology. Species cross-reactivity is determined by Western blot.

Specificity / Sensitivity

Beta-Catenin Antibody detects endogenous levels of total β-catenin protein.

Source / Purification

Polyclonal antibodies are produced by immunizing rabbits with a synthetic peptide (Blue Carrier-coupled) corresponding to residues surrounding Asp56 of human β-catenin. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of total cell extracts from 293 and NIH/3T3 cells, using β-Catenin Antibody (Amino-terminal Antigen).

Flow Cytometry

Flow Cytometry

Flow cytometric analysis of 293 cells, using β-Catenin Antibody (Amino-terminal Antigen) (blue) compared to a nonspecific negative control antibody (red).

IF-F

IF-F

Confocal immunofluorescence image of mouse colon labeled with β-Catenin Antibody (Amino-terminal Antigen) (red). Blue pseudocolor = DRAQ5™ (fluorescent DNA dye).


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).

  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.

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