Description

• General description: 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.
• Application: DTT has been used:as one of the reactants in the reduction and alkylation of αs1-Casein, the major allergen of cow′s milk.[1]as a component of medium for the demembranation and reactivation of spermatozoa.[2]to maintain stability of the enzyme as thiol effectively protects the active sites of the biocatalyst.[3]as a reducing agent to test the specificity of the reaction of N-Ethylmaleimide with sulfhydryl groups.[4]in proteomics analysis as in-solution protein digestion for mass spectrometry[5] as a buffer component for protein quantification, to prepare wash buffer, lysis buffer, sample buffer, and protein elution buffer[6][4]
• Biochem/physiol Actions: 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.[7]
• Features and Benefits: High-quality DTT (HPLC≥98%), (titration≥99.0%)Suitable for electrophoresis, proteomics analysis
• Other Notes: For additional information on our range of Biochemicals, please complete this form.