Used primarily as a highly selective covalent inhibitor in biochemical research, this compound targets specific enzymes by reacting with active site residues through its sulfonyl fluoride group. It is especially valuable in chemoproteomic studies for labeling and identifying reactive amino acids in proteins, aiding in the discovery of potential drug targets. Due to its ability to cross cell membranes, it is applied in live-cell experiments to probe enzyme function in native environments. Its chloro and methyl substitutions enhance stability and binding specificity, making it useful in developing activity-based protein profiling (ABPP) probes. Additionally, it serves as a key intermediate in synthesizing irreversible inhibitors for kinases and other ATP-binding proteins involved in signaling pathways linked to cancer and inflammatory diseases.