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HDAC1/HD1 [10E2]

Product group: Primary
Monoclonal/ Polyclonal: Monoclonal
Clone: 10E2
Host: Mouse
Isotype: IgG1
Application: ELISA, Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB)
Application notes: 50-200
Conjugation Type: Unconjugated
Lightchain type: Kappa
Reactivity: Human, Mouse, Rat
General notes: Localization: nucleus, cytoplasm.
Buffer: citrate pH6.0 or EDTA pH8.0
UNSPSC code: 12352203

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. HAT complexes interact with sequence-specific activator proteins to target specific genes. In addition to histones, HATs can acetylate non-histone proteins, suggesting multiple roles for these enzymes. In contrast, histone deacetylation promotes a “closed” chromatin conformation and typically leads to repression of gene activity. Mammalian histone deacetylases can be divided into three classes on the basis of their similarity to various yeast deacetylases. Class I (HDACs 1, 2, 3 and 8) proteins 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

HDAC1/HD1 [10E2]

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. HAT complexes interact with sequence-specific activator proteins to target specific genes. In addition to histones, HATs can acetylate non-histone proteins, suggesting multiple roles for these enzymes. In contrast, histone deacetylation promotes a “closed” chromatin conformation and typically leads to repression of gene activity. Mammalian histone deacetylases can be divided into three classes on the basis of their similarity to various yeast deacetylases. Class I (HDACs 1, 2, 3 and 8) proteins 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.