DITHIOTHREITOL (DTT)

Name: DL-1,4-Dithiothreitol
Synonym: Dithiothreitol; threo-1,4-Dimercapto-2,3-butanediol; Cleland's reagent; DTT
Struction:

Molecular formula: C4H10O2S2
Molecular weight: 154.25
CAS: 3483-12-3
EINECS: 222-468-7

Dithiothreitol (DTT), or Cleland's  Reagent, is an important chemical used to reduce disulfide bonds quantitatively and maintain monothiols in the reduced state.   At low concentrations, DTT stabilizes enzymes which possess free sulfhydryl groups and has been shown to restore activity lost by oxidation of these groups  in vitro.

DTT can readily permeate cell membranes allowing it to be used in pharmaceutical applications for high yield isolation and extraction of proteins.  At higher concentrations, DTT is an effective protein denaturant which cleaves disulfide linkages between cysteine groups in polypeptides.
The diverse attributes of DTT make it a valuable tool in stabilizing enzymes, antibodies, and growth factors, as well as being used for various research applications in protein structural analysis.

APPLICATIONS
1. Suitable for large-scale isolation and purification of protein
2. Important reagent in the study of enzymes, antibodies, and growth factors
3. Useful reagent for the protection o f thiol groups in organic synthesis
4. DTT reduction of thiocyanato masked synthon
5. DTT is a scavenger in solid phase peptide chemistry
6. DTT is most efficient reagent for thiolysis of dithiasuccinoyl protecting group
7. DTT reduction of azides
8. Protein chemistry
9. High level expression of recombinant proteins often results in protein aggregation and accumulation of inclusion bodies. In the processing of proteins with disulfide bonds, DTT is a key factor for the solubilization of these aggregates.  DTT cleaves disulfide bonds and maintains the respected cysteines in the reduced state.  The solubilization buffer generally includes6 Mguanidinium chloride or8 Murea as denaturant,100 mMTris HCl, and 10-100 mMDTT
10. The most prevalent method to refold protein is dilution of the solubilization buffer.  The final concentrations in the refolding buffer are 0-2 Mguandinium chloride or urea, 0-2 mMDTT and 10-100 mMTris-HCL. 
11. The buffer may contain refolding aids such as glutathione, oxidized glutathione, sulfobetaine, cyclodextrin, (+)-trans-1,2-bis(mercapto acetamido) cyclohexane, trimethylamine N-oxide, and other proteins, such as  molecular chaperones or folding enzymes.  In some cases of large scale protein folding and purification, DTT is also included to prevent undesirable oxidation.  

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