HDAC substrate is ideally suited to HDAC 4, 5, 7, 8 and 9 enzyme activity assays
Proprietary HDAC substrate
Histone deacetylases (HDACs) are highly conserved enzymes that regulate a diverse number of biological processes including gene expression, cell motility, nuclear translocation and oncogene stability. HDAC enzymes catalyze the removal of acetyl groups from the side chains of lysine residues, thus regulating protein structure and function. There are 18 human deacetylases which are presently the focus of broad biological and pharmaceutical investigation. The study of Class IIa enzymes (HDAC 4, 5, 7 and 9) - key targets for anti-inflammatory, neurologic and cardiovascular agents - has been challenging, as robust biochemical assays for these targets are not available.
Innovations and Advantages
Our proprietary HDAC substrate is ideally suited to HDAC 4, 5, 7, 8 and 9 enzyme activity assays and out-performs existing HDAC substrates.
When comparing our HDAC substrate with the commercially-available Fluor-de-Lys substrate (BIOMOL), our new substrate provides significantly greater coverage of the Class I and II HDACs, and allows for the first time the study of HDAC4, 5, 7 and 9 in a robust, miniaturized format.
The HDAC substrate allows (1) the sensitive and specific detection of Class IIa and HDAC 8 enzyme activity, (2) miniaturization to 384-well and 1536-well format for medicinal chemistry or HTS, and (3) the reduction of input enzyme to less than 1 ng/well.
It will be broadly utilized to study HDAC enzymes and the activity of new and established inhibitors by academic and industrial research groups.
Intellectual Property Status: Patent pending
Bradner JE, West N, Grachan ML, Greenberg EF, Haggarty SJ, Warnow T, Mazitschek R. 2010. Chemical phylogenetics of histone deacetylases. Nat Chem Biol. 6(3):238-243.
For further information, please contact:
Vivian Berlin, Director of Business Development
Reference Harvard Case #3146