AlternativeName: | Proteasome26SsubunitATPase2,26Sproteaseregulatorysubunit7,MSS1 |
Clone: | MSS1-104 |
Host: | Mouse |
Isotype: | IgG1 |
Immunogen: | RecombinanthumanRpt1protein. |
UniProtID: | P35998 |
Speciesreactivity: | Human,Mouse |
Specificity: | RecognizestheRpt1/S7subunitofthe19Sregulatorcomplex. |
Applications: | WB |
ApplicationNotes: | SingledimensionSDS-PAGEofproteasomalpreparationsfromavarietyofsourcesfollowedbyWesternblottinggivesasinglebandwitharelativemolecularweightofapproximately48kDa. Notsuitableforimmunoprecipitation. |
PurityDetail: | Purified. |
Formulation: | Liquid.InPBScontaining0.01%sodiumazide. |
Shipping: | ShippedonBlueIce |
LongTermStorage: | -20°C |
ScientificBackground: | Theproteasomeiswidelyrecognisedasthecentralenzymeofnon-lysosomalproteindegradation.ItisresponsIBLeforintracellularproteinturnoveranditisalsocriticallyinvolvedinmanyregulatoryprocessesand,inhighereukaryotes,inantigenprocessing.The26Sproteasomeisthekeyenzymeoftheubiquitin/ATP-dependentpathwayofproteindegradation.Thecatalyticcoreofthisunusuallylarge(2000kDa,450Åinlength)complexisformedbythe20Sproteasome,abarrelshapedstructureshownbyelectronmicroscopytocompriseoffourringseachcontainingsevensubunits.Basedonsequencesimilarity,allfourteen20Sproteasomalsubunitsequencesmaybeclassifiedintotwogroups,αandβ,eachgrouphavingdistinctstructuralandfunctionalroles.Theα-subunitscomprisetheouterringsandtheβ-subunitstheinnerringsofthe20Sproteasome.Observationsoftheeukaryoticproteasomeandanalysisofsubunitsequencesindicatethateachringcontainssevendifferentsubunits(α7β7β7α7)withamemberofeachsub-familyrepresentedineachparticle.Eachsubunitislocatedinauniquepositionwithintheα-orβ-rings. Inadditiontothe20Sparticle,the26Scomplexcontainsovertwentyadditionalproteins,ranginginmolecularweightfrom25to10kDa,locatedinadistinctcomplexcalledthe‘PA700proteasomeactivator’orthe‘19Scomplex’,andwhichdeterminessubstratespecificityandprovidesthemultipleenzymaticfunctionsnecessaryforproteolysisandviABIlity.Systematicanalysisofthesub-unitcomponentshaverevealedatleastsixmemberstobeATPasesbelongingtoanewfamilyofATPbindingproteins,togetherwithafurtherfifteensub-unitsthatlackthecapacitytobindATP,isopeptidasesandseveralotherproteinsthoughttoberesponsiblefortheunfoldingofaproteinsubstratepriortoinsertionintotheproteolyticcoreofthe20Sproteasome. |