As you know, the process of ubiquitin ligation and de-conjugation is emerging as a key regulator of cellular physiology. Research in this area, however, has been hindered by the lack of well characterized ubiquitin ligases, de-ubiquitinases, and facile assays for each. LifeSensors is proud to introduce the largest selection of DUBs and highly sensitive, novel isopeptidase assays (described by Nicholson, et al. (2008) Protein Sci.). 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.

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

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