Dl-Dithiothreitol
BioUltra, Molecular Biology, ≥99.5% (RT)
Receive your quote directly from the manufacturer.
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).
Application
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
- for peptide extraction and protein denaturation
- in sample preparation and reversal of formaldehyde crosslinks before mass spectrometry
- as a buffer component to extract synaptogliosome
