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Merck

A fluopol-ABPP HTS assay to identify PAD inhibitors.

Chemical communications (Cambridge, England) (2010-08-27)
Bryan Knuckley, Justin E Jones, Daniel A Bachovchin, Jessica Slack, Corey P Causey, Steven J Brown, Hugh Rosen, Benjamin F Cravatt, Paul R Thompson
要旨

Protein Arginine Deiminase (PAD) activity is dysregulated in numerous diseases, e.g., Rheumatoid Arthritis. Herein we describe the development of a fluorescence polarization-Activity Based Protein Profiling (fluopol-ABPP) based high throughput screening assay that can be used to identify PAD-selective inhibitors. Using this assay, streptonigrin was identified as a potent, selective, and irreversible PAD4 inactivator.

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製品内容

Sigma-Aldrich
ストレプトニグリン from Streptomyces flocculus, ≥98%