
- MultiSpecies
- USE-MeasureP450DemethylatingActivityWithoutAdditionstoP450Reaction
- SAMPLE-anyP450systemoranyBIOLOGicalsystemproducingFormaldehydeasdemethylationproduct
- SAMPLES/KIT-89inDuplicate
- CALIBRATED-MeasureFormaldehydeProduct
- STABILITY-Stable4˚CLiquidReagents
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TheDetectX®P450FluorescentActivitykitallowsactivitymeasurementofanydemethylatingP450systemWITHOUTanyadditionstothetheP450:Substratereaction.ThisassaymeasurestheformaldehydegeneratedbydemethylationandthesignalisreadAFTERtheP450reactionhasbeenterminated.Convenientplateassaywith30minutefluorescentsubstrateincubationanddetectionreadoutat510nm.Testedin3A4,2D6and2B4P450systemswitherythromycin,dextromethorphanorbenzphetamine.
ThecytochromeP450s(P450s)areasuperfamilyofhemecontainingenzymesthatdisplaytremendousdiversitywithregardtosubstratespecificityandcatalyticactivity.P450suseaplethoraofbothexogenousandendogenouscompoundsassubstratesintheirreactions.Usuallytheyformpartofmulticomponentelectrontransferreactions.CatalysisbytheeukaryoticP450enzymesinvolvesamultistepreactioncyclethatincludestwostepsinwhichelectrontransferisaccomplishedfromaredoxpartner.Thediflavinprotein,NADPHcytochromeP450reductasecontainsbothFADandFMNandcantransferbothelectronsneededforthecatalyticcycle.InsomeP450reactions,thesecondelectronofthereactioncyclealsocanbedeliveredbycytochromeb5.TheP450enzymesandcofactorsofthemammaliandrug-metabolizingsystemareembeddedinthemembraneoftheendoplasmicreticulum.TheP450splayacrucialroleinthedevelopmentofnewdrugentitiesasdruginteractionscommonlyinhibitcytochromeP450activities.
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