|Reactivity||Human Mouse Rat|
|Tested applications||WB IHC IF IP CHIP|
|Recommended Dilution||WB 1:500 - 1:2000
IHC 1:50 - 1:200
IF 1:50 - 1:200
IP 1:50 - 1:200
ChIP 1:20 - 1:100|
|Observed MW||Refer to Figures|
|Immunogen||A synthetic peptide of human HDAC4|
|Storage Buffer||Store at -20℃. Avoid freeze / thaw cycles.
Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3.|
Western blot analysis of extracts of various cell lines, using HDAC4 antibody.
Immunofluorescence analysis of A549 cell using HDAC4 antibody. Blue: DAPI for nuclear staining.
Acetylation of the histone tail causes chromatin to adopt an "open" conformation, allowing increased accessibility of transcription factors to DNA. The identification of histone acetyltransferases (HATs) and their large multiprotein complexes has yielded important insights into how these enzymes regulate transcription (1,2). HAT complexes interact with sequence-specific activator proteins to target specific genes. In addition to histones, HATs can acetylate nonhistone proteins, suggesting multiple roles for these enzymes (3). In contrast, histone deacetylation promotes a "closed" chromatin conformation and typically leads to repression of gene activity (4). Mammalian histone deacetylases can be divided into three classes on the basis of their similarity to various yeast deacetylases (5). Class I proteins (HDACs 1, 2, 3, and 8) are related to the yeast Rpd3-like proteins, those in class II (HDACs 4, 5, 6, 7, 9, and 10) are related to yeast Hda1-like proteins, and class III proteins are related to the yeast protein Sir2. Inhibitors of HDAC activity are now being explored as potential therapeutic cancer agents (6,7).
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