Cell Signaling Technology

Product Pathways - Chromatin Regulation

Histone Deacetylase 4 (HDAC4) Antibody #2072

Applications Reactivity MW (kDa) Source
W H M R 140 Rabbit

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

Specificity / Sensitivity

Histone Deacetylase 4 (HDAC4) Antibody detects endogenous levels of total HDAC4 protein. This antibody detects only HDAC4 protein; it does not cross-react with other HDAC proteins.

Source / Purification

Polyclonal antibodies are produced by immunizing rabbits with a synthetic peptide (KLH-coupled) corresponding to residues surrounding amino acid 10 of human HDAC4. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell types or tissue using Histone Deacetylase 4 (HDAC4) Antibody.

Background

Acetylation of the histone tail causes chromatin to adopt an "open" conformation, allowing trans factors increased accessibility 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 non-histone 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 (HDACs 1, 2, 3 and 8) proteins 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).

  1. Marmorstein, R. et al. (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, 5540-5543.
  4. Cress, S.D. and Seto, E. (2000) J. Cell. Physiol. 184, 1-16.
  5. Gray, S.G. and Ekstrom, T.J. (2001) Exp. Cell Res. 262, 75-83.
  6. Thiagalingam, S. et al. (2003) Ann. N. Y. Acad. Sci. 983, 84-100.
  7. Viguishin, D.M. and Coombes, R.C. (2004) Curr. Cancer Drug Targets 4, 205-218.

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