DL-Dithiothreitol (DTT) is widely used in biochemistry and molecular biology as a reducing agent. It is particularly effective in breaking disulfide bonds within and between proteins, which helps in denaturing proteins for analysis or in maintaining them in a reduced state during experiments. DTT is commonly employed in techniques such as SDS-PAGE to ensure proteins remain unfolded and separated by size. It is also used in nucleic acid research to stabilize enzymes like reverse transcriptase and DNA polymerase by preventing oxidation. Additionally, DTT plays a role in cell culture applications, where it helps maintain the redox environment necessary for cell viability. Its ability to reduce disulfide bonds makes it valuable in studying protein structure, function, and interactions.