Description

• General description: 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: 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]
• Biochem/physiol Actions: 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]
• Features and Benefits: BioUltra grade powder suitable for molecular biology DNase, RNase, phosphatase, and protease-free insoluble matter, passes the filter test Stringently tested and free from trace metals
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