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 (p300/CBP-associated factor), p300/CBP, HAT1, 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.
Fig1: Western blot analysis of HDAC7 on different lysates using anti-HDAC7 antibody at 1/1,000 dilution. Positive control: Lane 1: A549 Lane 2: Human brain
Application
Fig2: Flow cytometric analysis of K562 cells with HDAC7 antibody at 1/50 dilution (red) compared with an unlabelled control (cells without incubation with primary antibody; black). Alexa Fluor 488-conjugated goat anti rabbit IgG was used as the secondary antibody
Positive Control
A549, human brain tissue.
Application Notes
WB:1:1,000-1:2,000 FC:1:50-1:100
Additional Information
Form
Liquid
Storage Instructions
Store at +4℃ after thawing. Aliquot store at -20℃ or -80℃. Avoid repeated freeze / thaw cycles.
