HDAC2 Antibody

2540:

Immunofluorescence , Western Blotting

HDAC2 Antibody detects endogenous levels of HDAC2 protein. The antibody does not cross-react with other HDAC proteins.

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the carboxy terminus of the human HDAC2 protein. Antibodies are purified by peptide affinity chromatography.

Western Blotting

Western blot analysis of various cell types using HDAC2 Antibody.

IF-IC

Confocal immunofluorescent analysis of COS cells using HDAC2 Antibody (green). Actin filaments have been labeled with Alexa Fluor^® 555 phalloidin (red).

Acetylation of the histone tail causes chromatin to adopt an "open" conformation, allowing increased accessibility of transcription factors to DNA. The identification of histone acetyltransferases (HATs) and their large multiprotein complexes has yielded important insights into how these enzymes regulate transcription (1,2). HAT complexes interact with sequence-specific activator proteins to target specific genes. In addition to histones, HATs can acetylate nonhistone proteins, suggesting multiple roles for these enzymes (3). In contrast, histone deacetylation promotes a "closed" chromatin conformation and typically leads to repression of gene activity (4). Mammalian histone deacetylases can be divided into three classes on the basis of their similarity to various yeast deacetylases (5). Class I proteins (HDACs 1, 2, 3, and 8) are related to the yeast Rpd3-like proteins, those in class II (HDACs 4, 5, 6, 7, 9, and 10) are related to yeast Hda1-like proteins, and class III proteins are related to the yeast protein Sir2. Inhibitors of HDAC activity are now being explored as potential therapeutic cancer agents (6,7).

HDAC1 and HDAC2 are highly homologous and are involved in histone deacetylation, chromatin remodeling and transcriptional repression (8-10). Both proteins are found together in numerous complexes including the nucleosome remodeling and deacetylation complex (NuRD), MeCP1, and the mSin3A corepressor complex.

1. Marmorstein, R. (2001) Cell Mol Life Sci 58, 693-703.
2. Gregory, P.D. et al. (2001) Exp Cell Res 265, 195-202.
3. Liu, Y. et al. (2000) Mol Cell Biol 20, 5540-53.
4. Cress, W.D. and Seto, E. (2000) J Cell Physiol 184, 1-16.
5. Gray, S.G. and Ekström, T.J. (2001) Exp Cell Res 262, 75-83.
6. Thiagalingam, S. et al. (2003) Ann. N.Y. Acad. Sci. 983, 84-100.
7. Vigushin, D.M. and Coombes, R.C. (2004) Curr. Cancer Drug Targets 4, 205-218.
8. Zhang, Y. et al. (1999) Genes Dev. 13, 1924-1935.
9. Ng, H.H. et al. (1999) Nat. Genet. 23, 58-61.
10. Zhang, Y. et al. (1997) Cell 89, 357-364.

• Zhang, Z. et al. (2011) Nat Med 17, 1448-55. Applications: ChIP

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For Research Use Only. Not For Use In Diagnostic Procedures.