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Updated: Jan 24, 2026

Photoconversion of Purified Fluorescent Proteins and Dual-probe Optical Highlighting in Live Cells
Published on: June 26, 2010
Design and synthesis of fluorescent activity probes for protein phosphatases
Garrett R Casey1, Jon R Beck1, Cliff I Stains2
1Department of Chemistry and Nebraska Center for Integrated Biomolecular Communication, University of Nebraska-Lincoln, Lincoln, NE, United States.
Abstract:
Protein phosphatases act in concert with protein kinases to regulate and maintain the phosphoproteome. However, the catalog of chemical tools to directly monitor the enzymatic activity of phosphatases has lagged behind their kinase counterparts. In this chapter, we provide protocols for repurposing the phosphorylation-sensitive sulfonamido-oxine fluorophore known as Sox to afford direct activity probes for phosphatases. With validated activity probes in-hand, inhibitor screens can be conducted with recombinant enzyme and the role of phosphatases in cell signaling can be investigated in unfractionated cell lysates.
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