Product Pathways - Chromatin Regulation / Epigenetics
HDAC4 (D15C3) Rabbit mAb #7628
PhosphoSitePlus® protein, site, and accession data: HDAC4
| Applications | Reactivity | Sensitivity | MW (kDa) | Isotype |
|---|---|---|---|---|
| W IP | H M R Mk | Endogenous | 140 | Rabbit IgG |
Applications Key:
W=Western Blotting
IP=Immunoprecipitation
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
HDAC4 (D15C3) Rabbit mAb recognizes endogenous levels of total HDAC4 protein. The antibody may cross-react with HDAC5.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a recombinant protein specific to the amino terminus of human HDAC4 protein.
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).
- 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.
Application References
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For Research Use Only. Not For Use In Diagnostic Procedures.