Eosin Y as an internal standard for a plate reader-based quantitation of a histone deacetylase substrate.
Ongoing interest in histone deacetylase (HDAC) inhibitors as potential anticancer drugs and mechanistic tools for the study of gene regulation is driving the improvement of assay techniques for the determination of HDAC activity. We previously reported the first non-isotopic substrate for HDAC. A plate reader-based determination of the substrate conversion utilized a boraindacene as an internal standard which is no longer commercially available. We report here that Eosin Y is a suitable replacement for that purpose, leading to a validated HDAC assay with increased throughput.
Heltweg
Birgit
B
Department of Pharmaceutical and Medicinal Chemistry, Westfälische Wilhelms-Universität Münster, Münster, Germany.
Jung
Manfred
M
D000970:Antineoplastic Agents / Q000494:pharmacology*; D002138:Calibration; D004354:Drug Screening Assays, Antitumor; D004791:Enzyme Inhibitors / Q000494:pharmacology*; D004801:Eosine Yellowish-(YS) / Q000737:chemistry*; D005456:Fluorescent Dyes / Q000737:chemistry*; D056572:Histone Deacetylase Inhibitors; D006655:Histone Deacetylases / Q000378:metabolism*; D007700:Kinetics; D012015:Reference Standards; D015203:Reproducibility of Results
D000970:Antineoplastic Agents; D004791:Enzyme Inhibitors; D005456:Fluorescent Dyes; D056572:Histone Deacetylase Inhibitors; D006655:Histone Deacetylases; D004801:Eosine Yellowish-(YS)