Human Histone Deacetylase (HDAC) Class I
Nucleic and amino acid sequences of human Class I HDACs
Histone deacetylases (HDAC) are a class of enzymes that remove acetyl groups from an epsilon-N-acetyl lysine amino acid on a histone. The first human HDAC was discovered and cloned by the Schreiber laboratory. HDACs are members of an enzyme family conserved in animals, plants, fungi and bacteria. There are three classes of HDACs in humans. Class I enzymes (HDACs 1, 2, 3 and 8) are ubiquitously expressed, predominantly nuclear, and mainly function as transcriptional corepressors. Class II enzyme (HDACs 4, 5, 6, 7, 9 and 10) distribution is more tissue specific, suggesting distinct functions in cellular differentiation and developmental processes.
Histone acetylation plays an important role in the regulation of gene expression. Hyperacetylated chromatin is transcriptionally active, and hypoacetylated chromatin is silent. Also, HDACs interact with a number of non-histone proteins that include transcription factors and co-regulators. HDACs play important roles in a variety of biological pathways, such as those involve in:
• Human diseases: e.g. cancers; chronic myeloid leukemia
• Cellular processes: e.g. cell growth and death; cell cycle
• Environmental information processing: e.g. signal transduction; notch signaling pathway
Innovations and Advantages
Recombinant HDAC proteins are used in biochemical in vitro assays, for raising antibodies against specific HDAC, and as in vitro protein targets in drug discovery approaches towards new HDAC inhibitors.
Non-exclusive research-use license is available for the intellectual properties covering the nucleic and amino acid sequences of human class I HDACs (HDACs 1, 2, 3 and 8). Please refer to case HU 1675 for class II HDACs.
Intellectual Property Status Issued and pending patent applications.
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Hassig, Christian A.
Jamison, Timothy F.
Schreiber, Stuart L.
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Reference Harvard Case #1250