Phospho-HDAC2 (Ser394) (E8O2Z) Rabbit mAb (Alexa Fluor® 647 Conjugate) #61458
- F
Supporting Data
| REACTIVITY | H M R Mk |
| SENSITIVITY | Endogenous |
| MW (kDa) | |
| Source/Isotype | Rabbit IgG |
Application Key:
- F-Flow Cytometry
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- Mk-Monkey
Product Information
Product Description
Product Usage Information
| Application | Dilution |
|---|---|
| Flow Cytometry (Fixed/Permeabilized) | 1:50 |
Storage
Protocol
Specificity / Sensitivity
Phospho-HDAC2 (Ser394) (E8O2Z) Rabbit mAb (Alexa Fluor® 647 Conjugate) recognizes endogenous levels of HDAC2 protein only when phosphorylated at Ser394.
Species Reactivity:
Human, Mouse, Rat, Monkey
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser394 of human HDAC2 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).
Ser394 is phosphorylated by CK2, which promotes enzymatic activity and regulates complex formation (8).
- 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, 205-18.
- Tsai, S.C. and Seto, E. (2002) J Biol Chem 277, 31826-33.
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