1,4-dithiothreitol

1,4-Dithiothreitol (DTT) is a small molecule reducing agent widely used in biochemical and molecular biology research. Its primary function is to protect thiol (SH) groups in proteins and other molecules by preventing their oxidation and to reduce disulfide bonds to free thiols. DTT achieves this through its low redox potential (−0.33 V at pH 7), which allows it to maintain SH-groups in the reduced state more effectively than similar agents like 2-mercaptoethanol. Upon oxidation, DTT forms a stable six-membered ring via an intramolecular disulfide bond. This property makes it especially useful for enzyme isolation and purification as well as for reactivation of enzymes that require reduced cysteine residues for activity[1][2][8]. While primarily used as a laboratory reagent rather than a therapeutic drug, there are rare reports of experimental use in certain medical conditions such as nephropathic cystinosis[5].

Other names

dithiothreitol2,3-dihydroxy-1,4-dithiobutane