| 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. |



