DTTisfrequentlyusedtoreducethedisulfidebondsofproteinsand,moregenerally,topreventintramolecularandintermoleculardisulfidebondsfromformingbetweencysteineresiduesofproteins.However,evenDTTcannotreduceburied(solvent-inaccess
IBLe)disulfidebonds,soreductionofdisulfidebondsissometimescarriedoutunderdenaturingconditions(e.g.,athightemperatures,orinthepresenceofastrongdenaturantsuchas6Mguanidiniumchloride,8Murea,or1%sodiumdodecylsulfate).DTTisoftentimesusedalongwithsodiumdodecylsulfateinSDS-PAGEtofurtherdenatureproteinsbyreducingtheirdisulfidebondstoallowforbetterseparationofproteinsduringelectrophoresis.Becauseofthe
ABIlitytoreducedisulfidebonds,DTTcanbeusedtodenatureCD38onredbloodcells.Conversely,thesolventexposureofdifferentdisulfidebondscanbeassayedbytheirrateofreductioninthepresenceofDTT.DTTcanalsobeusedasanoxidizingagent.Itsprincipaladvantageisthateffectivelynomixed-disulfidespeciesarepopulated,incontrasttootheragentssuchasglutathione.Inveryrarecases,aDTTadductmaybeformed,i.e.,thetwosulfuratomsofDTTmayformdisulfidebondstodifferentsulfuratoms;insuchcases,DTTcannotcyclizesinceithasnosuchremainingfreethiols.