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    當前位置 ： Millipore >>> Millipore/15-101 | Akt phosphorylation Pathway Explorer MiniPack/15-101/3 vials/Pk
    Millipore/15-101 | Akt phosphorylation Pathway Explorer MiniPack/15-101/3 vials/Pk
    • Millipore/15-101 | Akt phosphorylation Pathway Explorer MiniPack/15-101/3 vials/Pk

    Millipore/15-101 | Akt phosphorylation Pathway Explorer MiniPack/15-101/3 vials/Pk

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    貨號: 15-101
    品牌: Millipore
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      • Description
        CatalogueNumber15-101
        BrandFamilyUpstate
        TradeName
        • Upstate
        DescriptionAktphosphorylationPathwayExplorerMiniPack
        AlternateNames
        • ProteinkinaseB
        • RAC-alphaserine/threonine-proteinkinase
        • racproteinkinasealpha
        • v-aktmurinethymomaviraloncogenehomolog1
        • murinethymomaviral(v-akt)oncogenehomolog-1
        BackgroundInformationPathwayExplorerAntibodyMiniPack:
        EachPathwayExplorerAntibodyMinipackcontainsthreerelatedantibodiesaspartofasignalingcascadeoracombinationoftotalandphosphorylatedformsofkeysignalingtargets.Eachofthethreeantibodiesare30%theoriginalpacksize.FullsizeversionsofeachofthePathwayExplorerantibodiesareavailableforsaleindividuallyunderthesamecatalognumberwiththeremovalof“SP”offofeachone(e.g.05-591SPcanbeorderedas05-591).

        Anti-Akt/PKB,PHDomain,
        cloneSKB1:
        Akt(proteinkinaseB),aserine/threoninekinase,hasemergedasacriticalenzymeinsignaltransductionpathwaysinvolvedincellproliferation,apoptosis,angiogenesis,anddiabetes.InmammalsthreeisoformsofAkt(α,β,γorAkt1,2,3)arereportedthatexhibitahighdegreeofhomology,butdifferslightlyinthelocalizationoftheirregulatoryphosphorylationsites.Aktαisthepredominantisoforminmosttissues,whereasthehighestexpressionofAktβisobservedintheinsulin-responsivetissues,andAktγisabundantinbraintissue.EachAktisoformiscomposedofthreefunctionallydistinctregions:anN-terminalpleckstrinhomology(PH)domainthatprovidesalipid-bindingmoduletodirectAkttoPIP3,acentralcatalyticdomain,andaC-terminalhydrophobicmotif.

        Anti-phospho-Akt(Thr308),
        clone50-1C-25orAnti-phospho-Akt1/PKBα(Ser473),clone11E6:
        Akt/PKBisaSer/ThrkinaseandamajorknowneffecterofthePI3Kinasepathway.ItisinvolvedinmultiplesignalingpathwaysthatrelatetomanyBIOLOGicalprocessesincludingmetabolism,apoptosis,cellcyclecontrol,angiogenesis,differentiation,andcellgrowthandproliferation.Inmammals,threeisoformsofAkt(Akt1/PKCα,Akt2/PKBβ,andAkt3/PKBγ)exists.Theyexhibitahighdegreeofhomology,butdifferslightlyinthelocalizationoftheirregulatoryphosphorylationsites.Akt1isthepredominantisoformthatisinmosttissuesandisthoughttohaveadominantroleingrowth,survival,embryonicdevelopment,andADIpocytedifferentiation.Akt2iscorrelatedwiththeregulationofglucosehomeostasisandisthepredominantisoformexpressedininsulin-responsivetissues.Akt3isabundantinbraintissue.EachAktisoformiscomposedofthreefunctionallydistinctregions:anN-terminalPleckstrinHomology(PH)domainthatprovidesalipid-bindingmodule,acentralcatalyticdomaincontainingThr308,andaC-terminalhydrophobicmotifcontainingSer473.TheactivationofAKTisdependentonadualregulatorymechanismthatrequiresbothitstranslocationtotheplasmamembraneanddualphosphorylationonThr308andSer473byPDK1andtheTORC2complex,respectively.

        *Seefullsizeversionsforcorrespondingreferences.
        ProductInformation
        Components
        • 05-591SPAnti-Akt/PKB,PHDomain,
          cloneSKB1
        • 05-802RSPAnti-phospho-Akt(Thr308),
          clone50-1C-25
        • 05-669SPAnti-phospho-Akt1/PKBα(Ser473),clone11E6
        Presentation3individualtubescontainingeitherAnti-Akt/PKB,PHDomain,cloneSKB1;Anti-phospho-Akt(Thr308),clone50-1C-25;orAnti-phospho-Akt1/PKBα(Ser473),clone11E6


        PropertiesEachvialis30%thesizeoftheparentcatalognumber
        StorageandShippingInformation
        Applications
        ApplicationThisAntibodypackcontainsAnti-Akt/PKBAntibody,PHDomain,Anti-phospho-AktAntibody(Thr308),Anti-phospho-Akt1/PKBαAntibody(Ser473).
        BiologicalInformation
        EntrezGeneNumber
        GeneSymbol
        • AKT
        • C-AKT
        • EC2.7.11.1
        • MGC99656
        • PKB
        • PKB-ALPHA
        • PRKBA
        • RAC
        • RAC-ALPHA
        • RAC-PK-alpha
        UniProtNumber
        UniProtSummaryFUNCTION:Generalproteinkinasecapableofphosphorylatingseveralknownproteins.PhosphorylatesTBC1D4.Signalsdownstreamofphosphatidylinositol3-kinase(PI(3)K)tomediatetheeffectsofvariousgrowthfactorssuchasplatelet-derivedgrowthfactor(PDGF),epidermalgrowthfactor(EGF),insulinandinsulin-likegrowthfactorI(IGF-I).Playsaroleinglucosetransportbymediatinginsulin-inducedtranslocationoftheGLUT4glucosetransportertothecellsurface.MediatestheantiapoptoticeffectsofIGF-I.Mediatesinsulin-stimulatedproteinsynthesis,partlybyplayingaroleinbothinsulin-inducedphosphorylationof4E-BP1andininsulin-inducedactivationofp70S6kinase.Promotesglycogensynthesisbymediatingtheinsulin-inducedactivationofglycogensynthase.
        CATALYTICACTIVITY:ATP+aprotein=ADP+aphosphoprotein.
        ENZYMEREGULATION:Threespecificsites,oneinthekinasedomain(Thr-308)andthetwootheronesintheC-terminalregulatoryregion(Ser-473andTyr-474),needtobephosphorylatedforitsfullactivation.
        SUBUNIT:InteractswithCENTG1isoform2(PIKE-A)inthepresenceofguaninenucleotides.TheC-terminusinteractswithCCDC88A/GRDNandTHEM4.InteractswithAKTIP.Interacts(viaPHdomain)withMTCP1,TCL1AANDTCL1B.InteractswithCDKN1B;theinteractionphosphorylatesCDKN1Bpromoting14-3-3bindingandcell-cycleprogression.
        SUBCELLULARLOCATION:Cytoplasm.Nucleus.Cellmembrane.Note=Nucleusafteractivationbyintegrin-linkedproteinkinase1(ILK1).NucleartranslocationisenhancedbyinteractionwithTCL1A.
        TISSUESPECIFICITY:Inallhumancelltypessofaranalyzed.
        DOMAIN:BindingofthePHdomaintothephosphatidylinositol3-kinasealpha(PI(3)K)resultsinitstargetingtotheplasmamembrane.
        DOMAIN:TheAGC-kinaseC-terminalmediatesinteractionwithTHEM4.
        PTM:PhosphorylationonThr-308,Ser-473andTyr-474isrequiredforfullactivity.Ser-473phosphorylationbytheRictor-mTorcomplexfavorsThr-308phosphorylationbyPDPK1.Ser-473phosphorylationisenhancedbyinteractionwithCENTG1isoform2(PIKE-A).Ser-473phosphorylationisenhancedinfocalcorticaldysplasiaswithTaylor-typeballooncells.
        PhysicochemicalInformation
        Dimensions
        MaterialsInformation
        MaterialsInformation
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