HDAC2 (phospho-S394) polyclonal antibody

In the intact cell, DNA closely associates with histones and other nuclear proteins to form chromatin. The remodeling of chromatin is believed to be a critical component of transcriptional regulation and a major source of this remodeling is brought about by the acetylation of nucleosomal histones. Acetylation of lysine residues in the amino-terminal tail domain of histone results in an allosteric change in the nucleosomal conformation and an increased accessibility to transcription factors by DNA. Conversely, the deacetylation of histones is associated with transcriptional silencing. Several mammalian proteins have been identified as nuclear histone acetylases, including GCN5, PCAF (for p300/CBP-associated factor), p300/CBP and the TFIID subunit TAF II p250. Mammalian HDAC1 (also designated HD1), HDAC2 (also designated mammalian RPD3) and HDAC3, all of which are related to the yeast transcriptional regulator Rpd3p, have been identified as histone deacetylases.

Notch Signaling, Nuclear Receptor Signaling, Cell Cycle Control G1 S Checkpoint, DNA Methylation, Epigenetic Writers and Erasers of Histone H3, Epigenetic Writers and Erasers of Histones H2A H2B and H4

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE) .

Western blot (WB) analysis of p-HDAC2 (S394) polyclonal antibody at 1:500 dilution Lane1:HEK293T cell lysate treated with UV Lane2:PC12 cell lysate treated with UV Lane3:Mouse kidney tissuel lysate Lane4:Rat liver tissue lysate