- 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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