ᴅʟ-Dithiothreitol, 1 X 1 g (D0632-1G)

Dithiothreitol (DTT) is a disulfide (SH) reducing agent found in proteins and in the amino acid cysteine. It reduces a disulfide bond by forming a six-membrane ring and initiating a thiol-disulfide interchange. It is almost 7-fold stronger reducing agent than βME, hence efficient in lower concentrations. 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). For additional information on our range of Biochemicals, please complete this form. Dithiothreitol (DTT) is extensively applied in chemical peptide synthesis and biochemical preparations of thiol proteins. It is also used in protein chemistry studies, such as protein folding and enzyme activity. It also acts as an enzyme stabilizer to stop DNA modification. DTT specifically mediates the thiol-disulfide interchange reaction to entirely reduce the intra- or inter-molecular disulfide bonds in biomolecules. This reaction results in the formation of thiols and the cyclic disulfide of DTT. High-quality DTT (HPLC≥98%), (titration≥99.0%)Suitable for electrophoresis, proteomics analysis

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