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Cosmo/Anti 20S Proteasome Subunit Alpha Type-2 mAb (Clone GC4/5)/100 µl/CAC-SZU-PS-M03
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Application:WB,IEMClonality:MonoclonalHost:MousePurification:Ig-PGReactivity:Plant,Fish,Yeast,Rat,Human,FrogRegulatingproteinstABIlityandturnoverisakeytaskinthecell.Besideslysosomes,ubiquitin‐mediatedproteasomaldegradationcomprisesthemajorproteolyticpathwayineukaryotes.Proteinsdestinedfordegradationbytheproteasomeareconjugatedbya‘tag’,aubiquitinchaintoalysine,throughanextensivelyregulatedenzymaticcascade.Theubiquitylatedproteinsaresubsequentlytargetedfordegradationbythe26Sproteasome,themajorproteolyticmachineryforubiquitylatedproteinsinthecell.Ubiquitylationcanbeconsideredasanothercovalentpost‐translationalmodificationandsignal,comparabletoacetylation,glycosylation,methylation,andphosphorylation.However,ubiquitylationhasmultiplerolesinadditiontotargetingproteinsfordegradation.Dependingonthenumberofubiquitinmoietiesandthelinkagesmade,ubiquitinalsoplaysanimportantroleinDNArepair,proteinsortingandvirusbudding.Unregulateddegradationofproteins,orabnormallystableproteins,interferewithseveralregulatorypathways,andtheubiquitin‐proteasomepathwayisaffectedinanumberofdiseases,suchasneurodegenerativediseases,cellularatrophiesandmalignancies.Therefore,dissectingtheubiquitin‐proteasomepathwayandidentifyingproteinsinvolvedinconjunctionwiththesignalsrequiredforspecificdegradationofcertainsubstrates,wouldhelpindevelopingnoveltherapeuticapproachestotreatdiseaseswheretheubiquitin‐proteasomepathwayisimpaired.[from:Roos‐MattjusP.andSistonenL.Theubiquitin‐proteasomepathway(2009)AnnalsofMedicine36(4):285-295]The26Sproteasomeisanessentialcomponentoftheubiquitin-proteolyticpathwayineukaryoticcellsandisresponsIBLeforthedegradationofmostcellularproteins.Itiscomposedofa20Sproteasomecatalyticcoreandregulatoryparticlesateitherend.Thesubunitsofthe20Sproteasomeareclassifiedintotwofamilies,αandβ.Ineukaryotes,the20Sproteasomecontainssevenα-typesubunitsandsevenβ-typesubunits.Thefourteensubunitsarearrangedinfourringsofsevenandformanα7β7β7α7structure.Thisantibodyrecognizesα2subunitofthe20Sproteasomefromallorganismstested,yeasttohumanandissuitableforimmuno-electronmicroscopy.References:1)Tokumoto,T.,Tokumoto,M.,Seto,K.,Horiguchi,R.,Nagahama,Y.,Yamada,S.,Ishikawa,K.,Lohka,M.J.1999.Disappearanceofanovelproteincomponentofthe26SproteasomeduringXenopusoocytematuration.ExpCellRes247,313-319..PubMed:100663582)Wakata,Y.,Tokumoto,M.,Horiguchi,R.,Ishikawa,K.,Nagahama,Y.,Tokumoto,T.2004.Identificationofalpha-typesubunitsoftheXenopus20Sproteasomeandanalysisoftheirchangesduringthemeioticcellcycle.BMCBiochem5,18.PubMed:156035923)Tokumoto,M.,Horiguchi,R.,Nagahama,Y.,Ishikawa,K.,Tokumoto,T.2000.Twoproteins,agoldfish20Sproteasomesubunitandtheproteininteractingwith26Sproteasome,changeinthemeioticcellcycle.EurJBiochem267,97-103.PubMed:10601855
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