DL-Dithiothreitol

Dithiothreitol (DTT) is a thiol-reducing reagent that quantitatively reduces disulfide (SH) groups in biological molecules. It specifically targets 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 less toxic than 2-mercaptoethanol. Typically, a seven-fold lower concentration of DTT (100 mM) is more efficient than that of 2-mercaptoethanol (5% v/v, 700 mM).

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).

DTT has been used:

• as an enzyme stabilizer to maintain exebacase stability[1]
• for peptide extraction and protein denaturation[2]
• in sample preparation and reversal of formaldehyde crosslinks before mass spectrometry[3]
• as a buffer component to extract synaptogliosome[4]

Dithiothreitol (DTT) is broadly used in chemical peptide synthesis and biochemical preparations of thiol proteins. Additionally, studies on protein folding and enzyme activity in protein chemistry make use of DTT. This reagent explicitly mediates the thiol-disulfide exchange reaction to completely reduce the intra-or between sub-atomic disulfide bonds in biomolecules. This reaction brings about the arrangement of thiols and the cyclic disulfide of DTT.[5]

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Isolation of RNA using guanidinium salts. Inclusion of a reductant enhances denaturation by breaking intramolecular protein disulfide bonds.[6]