This antibody is provided in phosphate-buffered solution, pH 7.2, containing 0.09% sodium azide and 50% glycerol.
Preparation:
The antibody was purified by antigen-affinity chromatography.
Storage & Handling:
Upon receipt, store frozen at -20° C.
Application:
WB
Recommended Usage:
Each lot of this antibody is quality control tested by Western blotting. Western blotting, suggested working dilution(s): Use 10 μl per 5 ml antibody dilution buffer for each mini-gel. It is recommended that the reagent be titrated for optimal performance for each application.
Jurkat nuclear extract was resolved by electrophoresis, transferred to nitrocellulose and probed with rabbit anti-HDAC2 antibody. Proteins were visualized using a donkey anti-rabbit secondary conjugated to HRP and a chemiluminescence detection system.
Description:
HDAC2 is a 55 kD class I histone deacetylase similar to yeast RPD3 protein. This nuclear protein operates in concert with histone acetyltransferases to control core histone acetylation in highly conserved lysine residues. HDAC activity has been associated with transcriptional repression and nucleosomal condensation. HDAC2 is modified by phosphorylation (casein kinase 2) and ubiquitination. HDAC2 has been reported to interact with the mSin3A co-repressor complex and the Daxx protein. The Poly6075 has been shown to be useful for Western blotting of human and mouse HDAC2.
Other Names:
Histone deacetylase 2
Structure:
Class I histone deacetylase family, similar to yeast RPD3 protein; 55 kD
Distribution:
Nuclear
Function:
Operates in concert with histone acetyltransferases to control core histone acetylation in highly conserved lysine residues
Regulation:
HDAC activity has been associated with transcriptional repression, nucleosomal condensation
Modification:
Phosphorylation by CK2, Ubiquitination
Interaction:
mSin3A co-repressor complex, Daxx
Antigen References:
1. Tong, J., et al., 1998. Nature 395:917. 2. Grunstein, M. 1997. Nature 389:349. 3. Wolffe, A., 1996. Science 272:371. 4. Lee, D., et al., 1993. Cell 72:73.
