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Millipore/AB9688 | Anti-Tau phospho Threonine 212 Antibody/AB9688/100 µL
  • Millipore/AB9688 | Anti-Tau phospho Threonine 212 Antibody/AB9688/100 µL

Millipore/AB9688 | Anti-Tau phospho Threonine 212 Antibody/AB9688/100 µL

價(jià)格: ￥4308.00 市場(chǎng)價(jià): 7180.00
貨號(hào): AB9688
品牌: Millipore
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    • Description
      CatalogueNumberAB9688
      BrandFamilyChemicon®
      TradeName
      • Chemicon
      DescriptionAnti-TauphosphoThreonine212Antibody
      ProductInformation
      FormatAffinityPurified
      StorageandShippingInformation
      Applications
      ApplicationDetectTauphosphoThreonine212usingthisAnti-TauphosphoThreonine212AntibodyvalidatedforuseinWB.
      KeyApplications
      • WesternBlotting
      BIOLOGicalInformation
      HostRabbit
      SpeciesReactivity
      • Human
      AntibodyTypePolyclonalAntibody
      EntrezGeneNumber
      EntrezGeneSummaryThisgeneencodesthemicrotubule-associatedproteintau(MAPT)whosetranscriptundergoescomplex,regulatedalternativesplicing,givingrisetoseveralmRNAspecies.MAPTtranscriptsaredifferentiallyexpressedinthenervoussystem,dependingonstageofneuronalmaturationandneurontype.MAPTgenemutationshavebeenassociatedwithseveralneurodegenerativedisorderssuchasAlzheimer"sdisease,Pick"sdisease,frontotemporaldementia,cortico-basaldegenerationandprogressivesupranuclearpalsy.
      GeneSymbol
      • MAPT
      • MTBT2
      • MAPTL
      • PHF-tau
      • tau
      • DDPAC
      • FTDP-17
      • MGC138549
      • MSTD
      • TAU
      • FLJ31424
      • MTBT1
      • PPND
      Modifications
      • Phosphorylation
      UniProtNumber
      UniProtSummaryFUNCTION:SwissProt:P10636#PromotesmicrotubuleassemblyandstABIlity,andmightbeinvolvedintheestablishmentandmaintenanceofneuronalpolarity.TheC-terminusbindsaxonalmicrotubuleswhiletheN-terminusbindsneuralplasmamembranecomponents,suggestingthattaufunctionsasalinkerproteinbetweenboth.Axonalpolarityispredeterminedbytaulocalization(intheneuronalcell)inthedomainofthecellbodydefinedbythecentrosome.TheshortisoformsallowplasticityoftheCytoskeletonwhereasthelongerisoformsmaypreferentiallyplayaroleinitsstabilization.
      SIZE:758aminoacids;78878Da
      SUBUNIT:InteractswithPSMC2throughSQSTM1(Bysimilarity).InteractswithSQSTM1whenpolyubiquitinated.
      SUBCELLULARLOCATION:Cytoplasm,cytosol.Cellmembrane.Note=Mostlyfoundintheaxonsofneurons,inthecytosolandinassociationwithplasmamembranecomponents.
      TISSUESPECIFICITY:Expressedinneurons.IsoformPNS-tauisexpressedintheperipheralnervoussystemwhiletheothersareexpressedinthecentralnervoussystem.DEVELOPMENTALSTAGE:Four-repeat(typeII)tauisexpressedinanadult-specificmannerandisnotfoundinfetalbrain,whereasthree-repeat(typeI)tauisfoundinbothadultandfetalbrain.
      DOMAIN:SwissProt:P10636Thetau/MAPrepeatbindstotubulin.TypeIisoformscontain3repeatswhiletypeIIisoformscontain4repeats.
      PTM:PhosphorylationatserineandthreonineresiduesinS-PorT-Pmotifsbyproline-directedproteinkinases(PDPK:CDC2,CDK5,GSK-3,MAPK)(only2-3sitesperproteinininterphase,seven-foldincreaseinmitosis,andinPHF-tau),andatserineresiduesinK-X-G-SmotifsbyMAP/microtubuleaffinity-regulatingkinase(MARK)inAlzheimerdiseasedbrains.Phosphorylationdecreaseswithage.Phosphorylationwithintau"srepeatdomainorinflankingregionsseemstoreducetau"sinteractionwith,respectively,microtubulesorplasmamembranecomponents.PhosphorylationonSer-610,Ser-622,Ser-641andSer-673inseveralisoformsduringmitosis.&Polyubiquitinated.RequiresfunctionalTRAF6andmayprovokeSQSTM1-dependentdegradationbytheproteasome(Bysimilarity).PHF-taucanbemodifiedbythreedifferentformsofpolyubiquitination."Lys-48"-linkedpolyubiquitinationisthemajorform,"Lys-6"-linkedand"Lys-11"-linkedpolyubiquitinationalsooccur.&GlycationofPHF-tau,butnotnormalbraintau.Glycationisanon-enzymaticpost-translationalmodificationthatinvolvesacovalentlinkagebetweenasugarandanaminogroupofaproteinmoleculeformingketoamine.Subsequentoxidation,fragmentationand/orcross-linkingofketoamineleadstotheproductionofadvancedglycationendproducts(AGES).GlycationmayplayaroleinstabilizingPHFaggregationleADIngtotangleformationinAD.
      DISEASE:SwissProt:P10636#InAlzheimerdisease,theneuronalcytoskeletoninthebrainisprogressivelydisruptedandreplacedbytanglesofpairedhelicalfilaments(PHF)andstraightfilaments,mainlycomposedofhyperphosphorylatedformsofTAU(PHF-TAUorADP-TAU).&DefectsinMAPTareacauseoffrontotemporaldementiaandparkinsonismlinkedtochromosome17(FTDP17)[MIM:600274,172700];alsocalledfrontotemporaldementia(FTD)orhistoricallytermedPickcomplex.Thisformoffrontotemporaldementiaischaracterizedbypreseniledementiawithbehavioralchanges,deteriorationofcognitivecapacitiesandlossofmemory.Insomecases,parkinsoniansymptomsareprominent.Neuropathologicalchangesincludefrontotemporalatrophyoftenassociatedwithatrophyofthebasalganglia,substantianigra,amygdala.Inmostcases,proteintaudepositsarefoundinglialcellsand/orneurons.&DefectsinMAPTareacauseofpallido-ponto-nigraldegeneration(PPND)[MIM:168610].Theclinicalfeaturesincludeocularmotilityabnormalities,dystoniaandurinaryincontinence,besidesprogressiveparkinsonismanddementia.&DefectsinMAPTareacauseofcorticobasaldegeneration(CBD).Itismarkedbyextrapyramidalsignsandapraxiaandcanbeassociatedwithmemoryloss.NeuropathologicfeaturesmayoverlapAlzheimerdisease,progressivesupranuclearpalsy,andParkinsondisease.&DefectsinMAPTareacauseofprogressivesupranuclearpalsy(PSP)[MIM:601104,260540];alsoknownasSteele-Richardson-Olszewskisyndrome.PSPischaracterizedbyakinetic-rigidsyndrome,supranucleargazepalsy,pyramidaltractdysfunction,pseudobulbarsignsandcognitivecapacitiesdeterioration.Neurofibrillarytanglesandgliosisbutnoamyloidplaquesarefoundindiseasedbrains.Mostcasesappeartobesporadic,withasignificantassociationwithacommonhaplotypeincludingtheMAPTgeneandtheflankingregions.Familialcasesshowanautosomaldominantpatternoftransmissionwithincompletepenetrance;geneticanalysisofafewcasesshowedtheoccurrenceoftaumutations,includingadeletionofAsn-613.&DefectsinMAPTmaybeacauseofhereditarydysphasicdisinhibitiondementia(HDDD)[MIM:607485].HDDDisafrontotemporaldementiacharacterizedbyprogressivecognitivedeficitswithmemorylossandpersonalitychanges,severedysphasicdisturbancesleadingtomutism,andhyperphagia.
      SIMILARITY:Contains4Tau/MAPrepeats.
      PhysicochemicalInformation
      Dimensions
      MaterialsInformation
      MaterialsInformation
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