CHOP-Reporter technology offers a rapid and robust in vitro assay for isopeptidase (deconjugating enzyme) activity. The concept behind the Ub/Ubl-CHOP-Reporter Deconjugating Assay is the attachment of Ub/Ubl to a reporter enzyme for catalytic activity. Upon conjugation of ubiquitin, the reporter is rendered catalytically inactive. Upon cleavage of the Ub/Ubl-reporter system by isopeptidase activity, the activated, free reporter subsequently acts upon its substrate. Thus, in the coupled assay, the signal generated by cleavage of the reporter enzyme’s substrate is a quantitative measure of isopeptidase activity.

For more information on the CHOP-Reporter technology, please refer to:

Nicholson, B, Leach, C.A., et al (2008). “Characterization of ubiquitin and ubiquitin-like-protein isopeptidase activities.” Protein Sci., 17: 1035-1043