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Reactivity | Human Mouse Rat |
Tested applications | WB IHC IF IP ChIP |
Recommended Dilution | WB 1:500 - 1:2000 IHC 1:50 - 1:100 IF 1:50 - 1:200 IP 1:50 - 1:200 ChIP 1:20 - 1:100 |
Calculated MW | 49kDa |
Observed MW | Refer to Figures |
Immunogen | Recombinant protein of human HDAC3 |
Storage Buffer | Store at -20℃. Avoid freeze / thaw cycles. Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3. |
Concentration | bfp |
Synonym | HD3; RPD3; RPD3-2; |
Western blot analysis of extracts of various cell lines, using HDAC3 antibody.
Immunohistochemistry of paraffin-embedded mouse liver using HDAC3 antibody at dilution of 1:100 (x40 lens).
Immunohistochemistry of paraffin-embedded human lung cancer using HDAC3 antibody at dilution of 1:100 (x40 lens).
Immunohistochemistry of paraffin-embedded human colon carcinoma using HDAC3 antibody at dilution of 1:100 (x40 lens).
Immunohistochemistry of paraffin-embedded human stomach using HDAC3 antibody at dilution of 1:100 (x40 lens).
Immunofluorescence analysis of MCF7 cell using HDAC3 antibody. Blue: DAPI for nuclear staining.
Chromatin immunoprecipitation analysis extracts of 293T cell line, using HDAC3 antibody and rabbit IgG. The amount of immunoprecipitated DNA was checked by quantitative PCR. Histogram was constructed by the ratios of the immunoprecipitated DNA to the input.
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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