SUMOylation, as a post-translational modification of proteins, plays essential regulatory roles in a variety of pathological conditions. In the dynamic process of SUMOylation and deSUMOylation, SENPs (SUMO-specific proteases), in charge of deconjugation of SUMO (small ubiquitin-related modifier) from substrate proteins, have recently been found to be potential therapeutic targets for cancer treatment. A reliable and practical assay is much needed to accelerate the discovery of SENPs inhibitors. We established a quantitative assay based on readily available SDS-PAGE-Coomassie system using RanGAP-SUMO as the substrate, thus avoiding the use of expensive fluorescent dyes or the error-prone fluorescent reporter. Its reproducibility and reliability were also evaluated in this report.
Xie, W., Wang, Z., Zhang, J., Wang, L., Zhao, Y., & Zhou, H. (2016). Development and evaluation of a highly reliable assay for SUMO-specific protease inhibitors. Bioorganic and Medicinal Chemistry Letters, 26(9), 2124–2128. https://doi.org/10.1016/j.bmcl.2016.03.080