DL-Dithiothreitol solution

Dithiothreitol (DTT), a thiol group protectant,[1] is an excellent reagent for preventing the oxidation of SH groups in proteins. DTT solution is a potent and versatile disulfide-reducing agent.[2] It reduces a disulfide bond by forming a six-membrane ring and initiating a thiol-disulfide interchange.

DL-dithiothreitol solution has been used:

• in the treatment of intestinal explants[3]
• in homogenate preparation of gill cells for enzymatic assays[4]
• in protein electrophoresis for western blotting[5]
• in transglutaminase activity[6]
• in sample buffer for SDS-PAGE[7]
• in Western Blot, as a lysis buffer component for single-nucleus RNA-sequencing[8]
• as a component of protein extraction buffer for cell lysis[8]

DL-dithiothreitol (DTT) is used in a chemical debonding technique, that helps to remove bacteria from biofilms.[9] It can change the structural stability of the GABA(B) (gamma-aminobutyric acid) receptor by disabling the disulfide bonds between four cysteine residues positioned in the GABA(B1(a)) receptor structure.[10]Dithiothreitol (DTT) is broadly utilized in synthetic peptide synthesis and biochemical arrangements of thiol proteins. It can also be used to study protein chemistry topics like enzyme activity and protein folding. DTT explicitly controls the thiol-disulfide exchange response to completely reduce the intra-or between sub-atomic disulfide bonds in biomolecules. Thiols and the cyclic disulfide of DTT are the products of this reaction.

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