Cell Signaling Technology

Product Pathways - Chromatin Regulation / Epigenetics

HDAC1 (10E2) Mouse mAb #5356

Applications Reactivity Sensitivity MW (kDa) Isotype
W IP IF-IC H M R Mk Endogenous 62 Mouse IgG1

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

Protocols

Specificity / Sensitivity

HDAC1 (10E2) Mouse mAb detects endogenous levels of total HDAC1 protein. The antibody does not cross-react with other HDAC proteins.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to the carboxy terminus of human HDAC1 protein.

Western Blotting

Western Blotting

Western blot analysis of extracts from HeLa, NIH/3T3, and H-4-II-E cells using HDAC1 (10E2) Mouse mAb.

IF-IC

IF-IC

Confocal immunofluorescent analysis of HeLa cells using HDAC1 (10E2) Mouse mAb (green). Actin filaments were labeled with DY-554 phalloidin (red).

Background

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).

  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.

Application References

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Companion Products

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

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