Product Pathways - Chromatin Regulation / Epigenetics
HDAC3 (7G6C5) Mouse mAb #3949
|W IP IF-IC||H M R Mk||Endogenous||49||Mouse IgG2a|
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
HDAC3 (7G6C5) Mouse mAb detects endogenous levels of total HDAC3 protein. The antibody does not cross-react with other HDAC proteins.
Source / Purification
Monoclonal antibody is produced by immunizing animals with recombinant human HDAC3 protein.
Western blot analysis of extracts from various cell lines using HDAC3 (7G6C5) Mouse mAb.
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).
HDAC3 is a nuclear and cytoplasmic protein that deacetylates both histone (H2A, H3, H4) and non-histone substrates (RelA, SRY, p53, MEF2, PCAF and p300/CBP) (8). HDAC3 deacetylase activity is stimulated by interactions with the N-CoR and SMRT co-repressor proteins. Together, these three proteins form a functional complex that represses transcription associated with nuclear hormone receptors and other transcription factors, including Rev-Erb, COUP-TF, DAX1, MAD and Pit-1 (8,9). Phosphorylation of HDAC3 on Ser424 by casein kinase 2 (CK2) also increases HDAC3 deacetylase activity (9). Subsequently, de-phosphorylation by protein phosphatase 4 (PP4) decreases HDAC3 activity (9).
- 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.
- Karagianni, P. and Wong, J. (2007) Oncogene 26, 5439-5449.
- Zhang, X. et al. (2005) Genes Dev. 19, 827-839.
- Li, M. et al. (2011) J Immunol 187, 2711-22. Applications: Western Blotting
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For Research Use Only. Not For Use In Diagnostic Procedures.