#10831 HDAC7 (E7O8V) Rabbit mAb
|HDAC7 (E7O8V) Rabbit mAb recognizes endogenous levels of total HDAC7 protein. This antibody does not cross-react with other HDAC proteins, including HDAC4 and HDAC5.|
|Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Gly60 of human HDAC7 protein.|
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Western blot analysis of extracts from various cell lines using HDAC7 (E7O8V) Rabbit mAb.
Immunoprecipitation of HDAC7 from HCT 116 cell extracts. Lane 1 is 10% input, lane 2 is Rabbit (DA1E) mAb IgG XP® Isotype Control #3900, and lane 3 is HDAC7 (E7O8V) Rabbit mAb. Western blot analysis was performed using HDAC7 (E7O8V) Rabbit mAb.
Confocal immunofluorescent analysis of HUVEC cells, untreated (left) or treated with TPA #4174 (10 ng/mL, 4 hr; right) to promote cytoplasmic accumulation, using HDAC7 (E7O8V) Rabbit mAb (green). Actin filaments were labeled with DyLight™ 554 Phalloidin #13054 (red). Cells were mounted in ProLong® Gold Antifade Reagent with DAPI #8961 (blue).
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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