DL-Dithiothreitol

Dithiothreitol (DTT) is an excellent reagent for maintaining SH groups in a reduced state in proteins. It initiates the thiol-disulfide exchange reaction to completely reduce the intra-or inter-molecular disulfide bonds in biomolecules. DTT specifically targets the disulfide bridge of the cross-linker N,N′-bis(acryloyl)cystamine to break apart the matrix of a polyacrylamide gel and sodium dodecyl polyacrylamide gel electrophoresis (SDS-PAGE). Hence, it is highly effective in use with buffers that quantitatively reduce disulfides. DTT is less pungent and less toxic in nature than 2-mercaptoethanol. It is also 7x more concentrated than beta-mercaptoethanol.

An excellent reagent for maintaining SH groups in reduced state; quantitatively reduces disulfides. DTT is effective in sample buffers for reducing protein disulfide bonds prior to SDS-PAGE. DTT can also be used for reducing the disulfide bridge of the cross-linker N,N′-bis(acryloyl)cystamine to break apart the matrix of a polyacrylamide gel. DTT is less pungent and is less toxic than 2-mercaptoethanol. Typically, a seven fold lower concentration of DTT (100 mM) is needed than is used for 2-mercaptoethanol (5% v/v, 700 mM).

DL-Dithiothreitol is used in protein samples to reduce the disulfide bonds before loading the sample onto the gel for Western Blot or SDS-PAGE[1][2] It has been used in the procedure of in situ hybridization of mRNA.[3][3]

It has been used:

• as a component for protein extraction in western blot analysis[4]
• to prepare sample lysis buffer for quantitative mass spectroscopy[5]
• as a kinase buffer component for enzyme-linked immunosorbent assay (ELISA)[6]

Dithiothreitol (DTT) is frequently utilized in biochemical preparations of thiol proteins and chemical peptide synthesis. DTT is also used in protein chemistry research on the folding of proteins and enzyme activity.[7]

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