Cell Signaling Technology

Product Pathways - Wnt / Hedgehog / Notch

LEF1 (C18A7) Rabbit mAb #2286

Applications Reactivity MW (kDa) Source Isotype
W IP F H M 25-58 kDa Rabbit IgG

Applications Key:  W=Western Blotting  IP=Immunoprecipitation  F=Flow Cytometry
Reactivity Key:  H=Human  M=Mouse
Species enclosed in parentheses are predicted to react based on 100% sequence homology. Species cross-reactivity is determined by Western blot.

Specificity / Sensitivity

LEF1 (C18A7) Rabbit mAb detects endogenous level of total LEF1 proteins, including the dominant negative forms due to the usage of alternative promoter.

Source / Purification

Monoclonal antibodies are produced by immunizing rabbits with a synthetic peptide (KLH-coupled) corresponding to residues surrounding Val282 of human LEF1.

Western Blotting

Western Blotting

Western blot analysis of total cell lysates from mouse thymocytes, DLD1 and HCT15 cells, using LEF1 (C18A7) Rabbit mAb.

Flow Cytometry

Flow Cytometry

Flow cytometric analysis of Jurkat cells, using LEF1 (C18A7) Rabbit mAb (blue) compared to a nonspecific negative control antibody (red).

Background

LEF1 and TCF are members of the high mobility group (HMG) DNA binding protein family of transcription factors which consists of the following: Lymphoid enhancer factor 1 (LEF1), T Cell Factor 1 (TCF1), TCF3 and TCF4 (1). LEF1 and TCF1 were originally identified as important factors regulating early lymphoid development (2) that act downstream in Wnt signaling. LEF1/TCF bind to Wnt response elements to provide a docking site for β-catenin, which translocates to the nucleus to promote the transcription of target genes upon activation of Wnt signaling (3). LEF1/TCF proteins are dynamically expressed during development and aberrant activation of the Wnt signaling pathway is involved in many types of cancers including colon cancer (4,5).

LEF1 has several isoforms due to alternative splicing. LEF1 also has an alternative promoter that is preferentially active in lymphocytes. The isoforms generated by this alternative promoter have no amino-terminal β-catenin binding domain, therefore, they may function in a dominant negative manner (6-8).

  1. Waterman, M.L. (2004) Cancer Metastasis Rev. 23, 41-52.
  2. Schilham, M.W. and Clevers, H. (1998) Semin. Immunol. 10, 127-132.
  3. Brantjes, H. et al. (2002) Biol. Chem. 383, 255-261.
  4. Reya, T. and Clevers, H. (2005) Nature 434, 843-850.
  5. Logan, C.Y. and Nusse, R. (2004) Annu. Rev. Cell Dev. Biol. 20, 781-810.
  6. Hovanes, K. et al. (2000) Nucleic Acids Res 28, 1994-2003.
  7. Hovanes, K. et al. (2001) Nat Genet 28, 53-7.
  8. Kobielak, A. et al. (2001) Acta Biochim Pol 48, 221-6.

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