Histone deacetylase (HDAC) enzymes play a critical role in normal gene-regulation events and the maintenance of homeostasis. However, their dysregulation has been implicated in a variety of disease states, including several forms of cancer, congestive heart failure, diabetes, inflammation, and neurological disorders. Because of the early success of first-generation HDAC inhibitors in both basic research and clinical applications, there is strong continuing interest in developing more potent and selective compounds.
Unfortunately, existing research tools for characterization of HDAC function suffer from poor sensitivity, detection interferences, or are time-consuming and expensive to apply. In this article, we describe a simple, robust, and sensitive bioluminescent assay method that measures the activity of various HDAC enzyme isoforms from recombinant or cell-based sources.