Product Pathways - Chromatin Regulation / Epigenetics
Histone Deacetylase 5 (HDAC5) Antibody #2082
|W IP IHC-P||H M R Mk||Endogenous||124||Rabbit|
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.
Specificity / Sensitivity
Histone Deacetylase 5 (HDAC5) Antibody detects endogenous levels of total HDAC5 protein. The antibody may cross-react with high levels of HDAC4 protein.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the carboxy-terminal sequence of human HDAC5. Antibodies are purified by protein A and peptide affinity chromatography.
Western blot analysis of extracts from various cell types using Histone Deacetylase 5 (HDAC5) Antibody.
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).
- Marmorstein, R. (2001) Cell Mol Life Sci 58, 693-703.
- Gregory, P.D. et al. (2001) Exp Cell Res 265, 195-202.
- Liu, Y. et al. (2000) Mol Cell Biol 20, 5540-53.
- Cress, W.D. and Seto, E. (2000) J Cell Physiol 184, 1-16.
- Gray, S.G. and Ekström, T.J. (2001) Exp Cell Res 262, 75-83.
- Thiagalingam, S. et al. (2003) Ann. N.Y. Acad. Sci. 983, 84-100.
- Vigushin, D.M. and Coombes, R.C. (2004) Curr. Cancer Drug Targets 4, 205-218.
- Wu, H. and Olson, E. (2002) Activation of the MEF2 transcription factor in skeletal muscles from myotonic mice. J. Clin. Invest. 109 (10), 1327-1333. Applications: Western Blotting
- Xia, S. et al. (2010) Development 137, 1075-84. Applications: Western Blotting
- Zhao, J.X. et al. (2011) J Biol Chem 286, 16426-34. Applications: IP Western Blotting
- Zhang, Z. et al. (2011) Nat Med 17, 1448-55. Applications: ChIP
Have you published research involving the use of our products? If so we'd love to hear about it. Please let us know!
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For Research Use Only. Not For Use In Diagnostic Procedures.