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Millipore/16-202A | Anti-phospho-Histone H2A.X (Ser139) Antibody, clone JBW301, FITC conjugate/16-202A/100 µg
  • Millipore/16-202A | Anti-phospho-Histone H2A.X (Ser139) Antibody, clone JBW301, FITC conjugate/16-202A/100 µg

Millipore/16-202A | Anti-phospho-Histone H2A.X (Ser139) Antibody, clone JBW301, FITC conjugate/16-202A/100 µg

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貨號(hào): 16-202A
品牌: Millipore
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    • Description
      CatalogueNumber16-202A
      BrandFamilyUpstate
      TradeName
      • Upstate
      DescriptionAnti-phospho-HistoneH2A.X(Ser139)Antibody,cloneJBW301,FITCconjugate
      AlternateNames
      • H2AXS139P
      • HistoneH2A.X(phosphoS139)
      • H2Ahistonefamily,memberX
      • H2AXhistone
      BackgroundInformationHistoneH2Aisoneofthe5mainhistoneproteinsinvolvedinthestructureofchromatinineukaryoticcells.FeaturingamainglobulardomainandalongNterminaltailH2Aisinvolvedwiththestructureofthenucleosomesofthe"beadsonastring"structure.
      ProductInformation
      FormatFITC
      Control
      • Staurosporine-treatedJurkatcells
      PresentationPurifiedFITC-conjugatedmousemonoclonalIgG1inbuffercontainingPBSwith0.05%sodiumazide.Frozensolution.
      StorageandShippingInformation
      StorageConditionsStablefor1yearatfromdateofreceipt.
      Applications
      ApplicationUseAnti-phospho-HistoneH2A.X(Ser139)Antibody,cloneJBW301,FITCconjugate(mousemonoclonalantibody)validatedinFC,ICCtodetectphospho-HistoneH2A.X(Ser139)alsoknownasH2AXS139P,H2AXhistone.
      KeyApplications
      • FlowCytometry
      • Immunocytochemistry
      ApplicationNotesImmunocytochemistry:2-4μg/mLofapreviouslotdetectedphospho-histoneH2A.Xinetoposide-treatedHeLacellsfixedwith95%ethanol/5%aceticacid(10minutes),followedby1%formaldehyde,0.25%Triton?X-100inTBS(5min.).
      BIOLOGicalInformation
      ImmunogenKLH-conjugated,syntheticpeptide(CKATQA[pS]QEY)correspondingtoaminoacids134-142ofhumanhistoneH2A.X.Theimmunizingsequencehas8identicalaminoacidsinyeastandmouse.CloneJBW301.
      EpitopeSer139
      ClonecloneJBW301
      ConcentrationPleaserefertotheCertificateofAnalysisforthelot-specificconcentration.
      HostMouse
      SpecificityRecognizesHistoneH2A.XphosphorylatedatSer139,MW15kDa.
      IsotypeIgG1
      SpeciesReactivity
      • Human
      SpeciesReactivityNoteHuman.
      Broadspeciescross-reactivityisexpectedbasedonconservationofsequencehomology.
      AntibodyTypeMonoclonalAntibody
      EntrezGeneNumber
      EntrezGeneSummaryHistonesarebasicnuclearproteinsthatareresponsIBLeforthenucleosomestructureofthechromosomalfiberineukaryotes.Twomoleculesofeachofthefourcorehistones(H2A,H2B,H3,andH4)formanoctamer,aroundwhichapproximately146bpofDNAiswrappedinrepeatingunits,callednucleosomes.Thelinkerhistone,H1,interactswithlinkerDNAbetweennucleosomesandfunctionsinthecompactionofchromatinintohigherorderstructures.ThisgeneencodesamemberofthehistoneH2Afamily,andgeneratestwotranscriptsthroughtheuseoftheconservedstem-loopterminationmotif,andthepolyAadditionmotif.
      GeneSymbol
      • H2AFX
      • H2AX
      • H2a/x
      • H2A/X
      • H2A.X
      Modifications
      • Phosphorylation
      PurificationMethodProteinGPurified
      UniProtNumber
      UniProtSummaryFUNCTION:SwissProt:P16104#VarianthistoneH2AwhichreplacesconventionalH2Ainasubsetofnucleosomes.NucleosomeswrapandcompactDNAintochromatin,limitingDNAaccessibilitytothecellularmachinerieswhichrequireDNAasatemplate.Histonestherebyplayacentralroleintranscriptionregulation,DNArepair,DNAreplicationandchromosomalstABIlity.DNAaccessibilityisregulatedviaacomplexsetofpost-translationalmodificationsofhistones,alsocalledhistonecode,andnucleosomeremodeling.Requiredforcheckpoint-mediatedarrestofcellcycleprogressioninresponsetolowdosesofionizingrADIationandforefficientrepairofDNAdoublestrandbreaks(DSBs)specificallywhenmodifiedbyC-terminalphosphorylation.
      SIZE:143aminoacids;15145Da
      SUBUNIT:ThenucleosomeisahistoneoctamercontainingtwomoleculeseachofH2A,H2B,H3andH4assembledinoneH3-H4heterotetramerandtwoH2A-H2Bheterodimers.Theoctamerwrapsapproximately147bpofDNA.InteractswithnumerousproteinsrequiredforDNAdamagesignalingandrepairwhenphosphorylatedonSer-140.TheseincludeMDC1,TP53BP1,BRCA1andtheMRNcomplex,composedofMRE11A,RAD50,andNBN.InteractionwiththeMRNcomplexismediatedatleastinpartbyNBN.AlsointeractswithDHX9/NDHIIwhenphosphorylatedonSer-140.
      SUBCELLULARLOCATION:Nucleus.DEVELOPMENTALSTAGE:SynthesizedinG1aswellasinS-phase.
      DOMAIN:SwissProt:P16104The[ST]-QmotifconstitutesarecognitionsequenceforkinasesfromthePI3/PI4-kinasefamily.
      PTM:PhosphorylatedonSer-140(toformgamma-H2AFX)inresponsetoDNAdoublestrandbreaks(DSBs)generatedbyexogenousgenotoxicagentsandbystalledreplicationforks,andmayalsooccurduringmeioticrecombinationeventsandimmunoglobulinclassswitchinginlymphocytes.PhosphorylationcanextenduptoseveralthousandnucleosomesfromtheactualsiteoftheDSBandmaymarkthesurroundingchromatinforrecruitmentofproteinsrequiredforDNAdamagesignalingandrepair.Widespreadphosphorylationmayalsoservetoamplifythedamagesignaloraidrepairofpersistentlesions.PhosphorylationofSer-140inresponsetoionizingradiationismediatedbybothATMandPRKDCwhiledefectsinDNAreplicationinduceSer-140phosphorylationsubsequenttoactivationofATRandPRKDC.DephosphorylationofSer-140byPP2AisrequiredforDNADSBrepair.Inmeiosis,Ser-140phosphorylationmayoccuratsynaptonemalcomplexesduringleptoteneasanATM-dependentresponsetotheformationofprogrammedDSBsbySPO11.Ser-140phosphorylationmaysubsequentlyoccursatunsynapsedregionsofbothautosomesandtheXYbivalentduringzygotene,downstreamofATRandBRCA1activation.Ser-140phosphorylationmayalsoberequiredfortranscriptionalrepressionofunsynapsedchromatinandmeioticsexchromosomeinactivation(MSCI),wherebytheXandYchromosomescondenseinpachytenetoformtheheterochromaticXY-body.Duringimmunoglobulinclassswitchrecombinationinlymphocytes,Ser-140phosphorylationmayoccuratsitesofDNA-recombinationsubsequenttoactivationoftheactivation-inducedcytidinedeaminaseAICDA.&MonoubiquitinationofLys-120byRING1andRNF2/RING2complexgivesaspecifictagforepigenetictranscriptionalrepression(Bysimilarity).
      SIMILARITY:BelongstothehistoneH2Afamily.
      MolecularWeight15kDa
      PhysicochemicalInformation
      Dimensions
      MaterialsInformation
      MaterialsInformation
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