
- MultiSpecies
- VERSATILE-Westernblotting,ImmunoassayandImmunoprecipitation
- PURE-SuppliedinPBSwithnocarrierprotein
OurAbX™CysteineMouseMonoclonalisproducedasaProteinApurifiedantibody.Itwillmeasurecysteine-proteincomplexesundernon-reducingconditions.
Amongseveralpostranslationalmodificationsknowntodate,cysteinylationhasreceivedrelativelyverylittleinterest.Cysteinylationhasbeenimplicatedintheregulationofimmunity,proteinkinaseCactivityandasaMarkerforutero-placentalinsufficiencyasmonitoredbyserumalbumincysteinylation.ProteinS-thiolationbylowmolecularweight(LMW)thiolspreventstheirreversIBLeoxidationofcysteineresiduesduringoxidativestressandplaysaroleintheredoxregulationofthiol-containingproteins.ManyGram-positivebacterialackglutathioneandsothenatureofS-thiolationintheseorganismsremainselusive.IntheGram-positivemodelorganismBacillussubtilis,cysteinerepresentsthemostabundantLMWthiol.OneofthemostobviousresponsesofB.subtilistooxidativestressisthestronginductionofcysteinebiosynthesisgenes.Althoughtheoriginsofthiseffectareunclear,itmaybeareflectionofconsumptionoffreecysteinebyoxidationtocystineandtheformationofmixeddisulfideswithproteins.