DTT is widely used in biochemistry and molecular biology as a reducing agent to break disulfide bonds within and between proteins. It helps in maintaining the reduced state of thiol groups, which is crucial for protein structure and function studies. In protein purification, DTT is often added to lysis buffers to prevent the formation of disulfide bonds that could interfere with the process. It is also used in electrophoresis techniques, such as SDS-PAGE, to ensure proteins remain in their reduced form for accurate analysis. Additionally, DTT plays a role in DNA sequencing and PCR by stabilizing enzymes and preventing oxidation. Its ability to reduce disulfide bonds makes it essential in studying protein folding, enzyme activity, and protein-protein interactions.