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Millipore/MABE171 | Anti-phospho-Histone H2A.X (Thr120) Antibody, clone 11F5.3/MABE171/100 µg
  • Millipore/MABE171 | Anti-phospho-Histone H2A.X (Thr120) Antibody, clone 11F5.3/MABE171/100 µg

Millipore/MABE171 | Anti-phospho-Histone H2A.X (Thr120) Antibody, clone 11F5.3/MABE171/100 µg

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貨號: MABE171
品牌: Millipore
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    • Description
      CatalogueNumberMABE171
      DescriptionAnti-phospho-HistoneH2A.X(Thr120)Antibody,clone11F5.3
      AlternateNames
      • HistoneH2A.X
      • H2A/X
      BackgroundInformationHistoneH2A.XisavariantofhistoneH2A,andissimilarlyassociatedwithgenomicDNA.However,histoneisstructurallydifferentfromothermembersoftheH2AfamilyinpossessingaC-terminaltailthatcontainstheSer139residuethatisphosphorylatedinresponsetobreaksindouble-strandedDNA.ThephosphorylationofH2A.XisarapidprocessthatismediatedbyATM/ATRproteins.
      ProductInformation
      FormatPurified
      Control
      • UntreatedAndUvTreatedHelaCellLysateWithAndWithoutPeptideBlock
      PresentationPurifiedmousemonoclonalIgG3κinbuffercontaining0.1MTris-Glycine(pH7.4),150mMNaClwith0.05%sodiumazide.
      StorageandShippingInformation
      StorageConditionsStablefor1yearat2-8°Cfromdateofreceipt.
      Applications
      ApplicationAnti-phospho-HistoneH2A.X(Thr120)Antibody,clone11F5.3isamousemonoclonalantibodyfordetectionofphospho-HistoneH2A.X(Thr120)alsoknownasHistoneH2A.X,H2A/X&hasbeenvalidatedinWB,DB.
      KeyApplications
      • WesternBlotting
      • DotBlot
      ApplicationNotesDotBlot(Specificity)Analysis:Arepresentativelotblockedphospho-HistoneH2A.X(Thr120)inunmodifiedandmodifiedHistones.
      BIOLOGicalInformation
      ImmunogenKLH-conjugatedlinearpeptidecorrespondingtoHistoneH2A.XphosphorylatedatThr120.
      EpitopePhosphorylatedThr120
      Clone11F5.3
      ConcentrationPleaserefertotheCertificateofAnalysisforthelot-specificconcentration.
      HostMouse
      SpecificityThisantibodyrecognizesHistoneH2A.XphosphorylatedatThr120.
      SpeciesReactivity
      • Human
      AntibodyTypeMonoclonalAntibody
      EntrezGeneNumber
      EntrezGeneSummaryHistonesarebasicnuclearproteinsthatareresponsIBLeforthenucleosomestructureofthechromosomalfiberineukaryotes.Twomoleculesofeachofthefourcorehistones(H2A,H2B,H3,andH4)formanoctamer,aroundwhichapproximately146bpofDNAiswrappedinrepeatingunits,callednucleosomes.Thelinkerhistone,H1,interactswithlinkerDNAbetweennucleosomesandfunctionsinthecompactionofchromatinintohigherorderstructures.ThisgeneencodesamemberofthehistoneH2Afamily,andgeneratestwotranscriptsthroughtheuseoftheconservedstem-loopterminationmotif,andthepolyAadditionmotif.
      GeneSymbol
      • H2Afx
      • H2Ax
      Modifications
      • Phosphorylation
      PurificationMethodProteinGPurified
      UniProtNumber
      UniProtSummaryFUNCTION:VarianthistoneH2AwhichreplacesconventionalH2Ainasubsetofnucleosomes.NucleosomeswrapandcompactDNAintochromatin,limitingDNAaccessibilitytothecellularmachinerieswhichrequireDNAasatemplate.Histonestherebyplayacentralroleintranscriptionregulation,DNArepair,DNAreplicationandchromosomalstABIlity.DNAaccessibilityisregulatedviaacomplexsetofpost-translationalmodificationsofhistones,alsocalledhistonecode,andnucleosomeremodeling.Requiredforcheckpoint-mediatedarrestofcellcycleprogressioninresponsetolowdosesofionizingrADIationandforefficientrepairofDNAdoublestrandbreaks(DSBs)specificallywhenmodifiedbyC-terminalphosphorylation.

      SUBUNITSTRUCTURE:ThenucleosomeisahistoneoctamercontainingtwomoleculeseachofH2A,H2B,H3andH4assembledinoneH3-H4heterotetramerandtwoH2A-H2Bheterodimers.Theoctamerwrapsapproximately147bpofDNA.InteractswithnumerousproteinsrequiredforDNAdamagesignalingandrepairwhenphosphorylatedonSer-140.TheseincludeMDC1,TP53BP1,BRCA1andtheMRNcomplex,composedofMRE11A,RAD50,andNBN.InteractionwiththeMRNcomplexismediatedatleastinpartbyNBN.AlsointeractswithDHX9/NDHIIwhenphosphorylatedonSer-140.InteractswithARRB2;theinteractionisdetectedinthenucleusuponOR1D2stimulation.

      SUBCELLULARLOCATION:Nucleus.Chromosome.

      DEVELOPMENTSTAGE:SynthesizedinG1aswellasinS-phase.

      DOMAIN:The[ST]-QmotifconstitutesarecognitionsequenceforkinasesfromthePI3/PI4-kinasefamily.

      POST-TRANSLATIONALMODIFICATION:PhosphorylatedonSer-140(toformgamma-H2AFXorH2AX139ph)inresponsetoDNAdoublestrandbreaks(DSBs)generatedbyexogenousgenotoxicagentsandbystalledreplicationforks,andmayalsooccurduringmeioticrecombinationeventsandimmunoglobulinclassswitchinginlymphocytes.PhosphorylationcanextenduptoseveralthousandnucleosomesfromtheactualsiteoftheDSBandmaymarkthesurroundingchromatinforrecruitmentofproteinsrequiredforDNAdamagesignalingandrepair.Widespreadphosphorylationmayalsoservetoamplifythedamagesignaloraidrepairofpersistentlesions.PhosphorylationofSer-140(H2AX139ph)inresponsetoionizingradiationismediatedbybothATMandPRKDCwhiledefectsinDNAreplicationinduceSer-140phosphorylation(H2AX139ph)subsequenttoactivationofATRandPRKDC.DephosphorylationofSer-140byPP2AisrequiredforDNADSBrepair.Inmeiosis,Ser-140phosphorylation(H2AX139ph)mayoccuratsynaptonemalcomplexesduringleptoteneasanATM-dependentresponsetotheformationofprogrammedDSBsbySPO11.Ser-140phosphorylation(H2AX139ph)maysubsequentlyoccursatunsynapsedregionsofbothautosomesandtheXYbivalentduringzygotene,downstreamofATRandBRCA1activation.Ser-140phosphorylation(H2AX139ph)mayalsoberequiredfortranscriptionalrepressionofunsynapsedchromatinandmeioticsexchromosomeinactivation(MSCI),wherebytheXandYchromosomescondenseinpachytenetoformtheheterochromaticXY-body.Duringimmunoglobulinclassswitchrecombinationinlymphocytes,Ser-140phosphorylation(H2AX139ph)mayoccuratsitesofDNA-recombinationsubsequenttoactivationoftheactivation-inducedcytidinedeaminaseAICDA.PhosphorylationatTyr-143(H2AXY142ph)byBAZ1B/WSTFdeterminestherelativerecruitmentofeitherDNArepairorpro-apoptoticfactors.PhosphorylationatTyr-143(H2AXY142ph)favorstherecruitmentofAPBB1/FE65andpro-apoptosisfactorssuchasMAPK8/JNK1,triggeringapoptosis.Incontrast,dephosphorylationofTyr-143byEYAproteins(EYA1,EYA2,EYA3orEYA4)favorstherecruitmentofMDC1-containingDNArepaircomplexestothetailofphosphorylatedSer-140(H2AX139ph).MonoubiquitinationofLys-120(H2AXK119ub)byRING1andRNF2/RING2complexgivesaspecifictagforepigenetictranscriptionalrepression.FollowingDNAdouble-strandbreaks(DSBs),itisubiquitinatedthrough"Lys-63"linkageofubiquitinmoietiesbytheE2ligaseUBE2NandtheE3ligasesRNF8andRNF168,leadingtotherecruitmentofrepairproteinstositesofDNAdamage.Monoubiquitinationandionizingradiation-induced"Lys-63"-linkedubiquitinationaredistinctevents.AcetylationatLys-37increasesinSandG2phases.ThismodificationhasbeenproposedtoplayaroleinDNAdouble-strandbreakrepair.

      SEQUENCESIMILARITIES:BelongstothehistoneH2Afamily.
      MolecularWeight~17kDaobserved
      PhysicochemicalInformation
      Dimensions
      MaterialsInformation
      MaterialsInformation
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