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 HDAC8, isolated from human kidney, is a histone deacetylase that shares homology to other HDACs but has different tissue distribution. HDAC8 is localized to the nucleus and plays a role in the development of a broad range of tissues and in the etiology of cancer.
Fig1: Western blot analysis of HDAC8 on K562 cells lysates using anti-HDAC8 antibody at 1/1,000 dilution.
Application
Fig2: Flow cytometric analysis of K562 cells with HDAC8 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
HUVEC, MCF-7, Hela, HepG2, human liver tissue, mouse liver tissue, mouse brain tissue, human lung 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.
