See our latest publication, “Biochemical Assay Development for Histone Methyltransferases Using a Transcreener-Based Assay for S-Adenosylhomocysteine” in Assay and Drug Development Technologies
Screening or profiling histone methyltransferases (HMTs) can often require challenging assay development. Their complex enzyme and substrate requirements compound the difficulties imposed by their unusual (read SLOW) kinetic properties. In a recent study published in Assay and Drug Development Technologies, BellBrook scientists Meera Kumar and Tom Zielinski summarized the optimization of assay conditions for a panel of 13 HMTs during development of the Transzyme Methyltransferase Assay Kits. Using purified, recombinant enzymes from Reaction Biology and BellBrook’s Transcreener EPIGEN assay, they identified optimal acceptor substrates and their concentrations, optimized detection reagents, determined initial velocity enzyme concentrations, and measured dose responses for some known inhibitors. One of the interesting findings was the variability in the activity observed with different nucleosome preparations.