Histone Deacetylase 7 (Phospho-S155) 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 HDAC7 is a histone deacetylase that interacts with the adaptor mSin3A. The interaction of HDAC7 with mSin3A suggests the association of multiple repression complexes of transcription factors.

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

Histone Deacetylase 7 (Phospho-S155) polyclonal antibody detects endogenous levels of Histone Deacetylase 7 protein only when phosphorylated at Ser155.

Western blot (WB) analysis of Histone Deacetylase 7 (Phospho-S155) polyclonal antibody at 1:500 dilution LaneA:HEK293T whole cell lysate LaneB:Hela whole cell lysate LaneC:U20S whole cell lysate LaneD:The Lung tissue lysate of Rat