Biochem/physiol Actions

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. 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.

Physical form

Clear and colorless frozen liquid solution

Preparation Note

Use a manual defrost freezer and avoid repeated freeze-thaw cycles. While working, please keep sample on ice.