Merck, D9779-5G, 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.