TPCK is widely used in biochemical research as a specific inhibitor for serine proteases, particularly chymotrypsin. It works by alkylating the histidine residue in the active site of the enzyme, effectively blocking its activity. This property makes TPCK a valuable tool for studying the role of chymotrypsin-like enzymes in various biological processes, including protein digestion, blood clotting, and immune responses. Additionally, TPCK is employed in cell culture studies to investigate apoptosis and cell signaling pathways, as it can inhibit proteases involved in these processes. It is also used in research on gene expression regulation, where proteases play a role, helping researchers identify key enzymes in these mechanisms. In drug discovery research, understanding TPCK's inhibition mechanism aids in designing effective and specific protease inhibitors for diseases such as cancer, infections, and neurological disorders. Furthermore, TPCK is utilized in laboratories to protect protein samples during purification and analysis by inhibiting degradative proteases. Its specificity and effectiveness in inhibiting serine proteases have made it a key reagent in enzymology and molecular biology research.