HDAC3 (Histone Deacetylase)

The nucleosomal histones can be modified through reversible acetylation by histone acetyltransferases (HATs) and deacetylases (HDACs). Acetylation and deacetylation of histone proteins alters chromosome structure and affects transcription factor access to DNA. HDAC3 has an open reading frame of 428 amino acids. HDAC3 shares 53% amino acid identity with HDAC1 and 52% with HDAC2 (1). Observations indicate that class II HDACs regulate transcription by bridging the enzymatically active NCOR2-HDAC3 complex and select transcription factors. All HDACs were found to be ubiquitously expressed in immune and non-immune tissues. In human myeloid leukemia THP-1 cells, HDAC3 transfection resulted in increased size, aberrant nuclear morphology and cell cycle G2/M cell accumulation. Functional activity of the expressed HDAC3 protein was confirmed in alpha-HDAC3 antibody immunoprecipitates by a histone deacetylase assay. Study suggests the participation of HDACs in cell cycle progression and activation (2).
The recombinant Flag tagged HDAC3 protein was isolated from Baculovirus strains that carried the coding sequence of the human HDAC3 protein under control of a T7 promoter.
Recombinant HDAC3 can be used 1) for in vitro function studies including transcription in the presence of co-factors suchas N-CoR; 2) for protein-protein interaction assay; and 3) for cell growth assay.
Purified protein is greater than 95% homogeneous based on SDS-PAGE analysis.
1 unit equals 1 nanogram of purified protein.
variable in different lots
1x dilution buffer A: 20 mM Tris-Cl (pH 8.0), 20% Glycerol, 100 mM KCl, 1 mM DTT and 0.2 mM EDTA
 
References:
1. Yang, et al., (1997) J. Biol. Chem. 272: 28001-28007
2. Dangond,F., et al., (1998) Biochem. Biophys. Res. Commun. 242 (3): 648-652