DTT; DL-Dithiothreitol; Cleland’s reagent; 1,4-Dithio-DLthreitol;threo-1,4-Dimercapto-2,3-butanediol; 1,4- bis(sulfanyl)butane-2,3-diol
Dithiothreitol (DTT), is a small-molecule redox reagent, known as Cleland's reagent, that forms a six-member ring with an internal disulfide bond. It has a redox potential of -0.33 V at pH 7. The reduction of typical disulfide bond proceeds by two sequential thiol-disulfide exchange reactions.
DTT is effective in buffers to reduce protein disulfide bonds prior to SDS-PAGE. It can protect protein sulfhydryls and restore enzyme activity lost by oxidation.
- For reducing or "deprotecting" agent for thiolated DNA
- For reducing disulfide bonds of proteins
- Used as an oxidizing agent
- Used as a component of medium for the demembranation and reactivation of spermatozoa
- Used to prevent intramolecular and intermolecular disulfide bonds from forming between cysteine residues of proteins
Additional Reading from AG Scientific:
- DTT (Dithiothreitol): Frequently Asked Questions
- DTT (Dithiothreitol): Applications You Must Know
- TCEP HCl vs. DTT: Preferred Reducing Agents
Research or further manufacturing use only, not for food or drug use.