HDAC4 (N-terminus) monoclonal 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, p300/CBP, PCAF (p300/CBPassociated factor), HAT1 and the TFIID subunit TAF II p250. Mammalian HDAC1 (also designated HD1), HDAC2 (also designated RPD3) and HDAC3-6 have been identified as histone deacetylases.

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

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