Used as a highly effective sulfonylating agent in organic synthesis, particularly in the modification of peptides and proteins. It readily reacts with nucleophilic amino acid residues such as serine, threonine, and tyrosine, making it valuable in proteomics research for identifying active sites in enzymes. Commonly employed in chemical biology for activity-based protein profiling (ABPP), enabling the study of enzyme function in complex biological systems. Its stability and selectivity under physiological conditions make it suitable for labeling and inhibiting serine hydrolases and other nucleophilic enzyme families. Also utilized in the development of covalent inhibitors in drug discovery due to its ability to form irreversible bonds with target proteins.