Desalting and Gel Filtration Chromatography - TW

Desalting and buffer exchange use gel filtration chromatography (or size-exclusion chromatography) to separate soluble macromolecules from smaller molecules ... PopularApplications&TechniquesShopAllProductsServicesSupport Signin QuickOrder     Search ThermoFisherScientific SearchAll Search Home›LifeSciences›ProteinBiology›ProteinBiologyLearningCenter›ProteinBiologyResourceLibrary›PierceProteinMethods›DesaltingandGelFiltrationChromatographyDesaltingandGelFiltrationChromatographySeeNavigation ProteinBiologyResourceLibrary PierceProteinMethods Desaltingandbufferexchangeusegelfiltrationchromatography(orsize-exclusionchromatography)toseparatesolublemacromoleculesfromsmallermolecules.Whenanaqueoussolutionisusedtotransportthesamplethroughthecolumn,thetechniqueisreferredtoasgel-filtrationchromatography.Desaltingandbufferexchangearetwoofthemostwidelyusedgelfiltrationchromatographyapplications,andbothcanbeperformedusingthesamematerials. PagecontentsIntroductionHowgelfiltrationchromatographyworksParametersofgelfiltrationchromatographyMethodsforgelfiltrationchromatographyViewandselectproductsZebaDesaltingProductSelectionGuideDesaltingColumnsSpinCupsandColumnsCentrifugeColumns Introduction Indesaltingandbufferexchange,themacromolecularcomponentsofasamplearerecoveredinthebufferusedtopre-equilibratethegel-filtrationmatrixthroughwhichthesampleisprocessed.Themethodiscommonlyreferredtoasdesaltingwhenthegoalistoremovebuffersaltsfromasampleinexchangeforwater(withwaterusedtopre-equilibratethegel-filtrationresin).Bufferexchangeisthetermusedwhenonesetofbuffersaltinasampleisexchangedforanotherset.Applicationsfordesaltinginclude:RemovingsaltsfromproteinsolutionsRemovingphenolorunincorporatednucleotidesfromnucleicacidpreparationsSeparatingexcesscrosslinking,labelingorderivatizationreagentsfromconjugatedproteinsBufferexchangeisusedtoplaceaproteinsolutionintoamoreappropriatebufferbeforesubsequentapplicationssuchas:ElectrophoresisIonexchange(IEX)Affinitychromatography(AC)Passageofaproteinsamplethroughacolumnofporousresinfacilitatesbufferexchangeanddesalting. Smallmoleculesintheoriginalsample(red)enterthebeadpores,therebytakingalongerandslowerpaththroughthecolumnthantheprotein(yellow).Asaresulttheproteinseparatesfromtheoriginalbuffersaltsandexchangesintothecolumnbuffer.Gelfiltrationchromatographyisusefulformanyofthesamepurposesasdialysis,becausebothmethodsarebasedonsimilarrangesofmolecularweightcut-off(MWCO)limitsthatexcludemoleculesbasedonsize.Comparedtodialysis,gelfiltrationhastheadvantageofspeed(afewminutesvs.hoursfordialysis),whichisnecessaryincertainexperimentalsituations.Forexample,reducedpeptidesmustbedesaltedquicklytoremovereductantandinitiatesubsequentsulfhydryl-reactionproceduresbeforeoxidationbacktodisulfidesoccurs.Also,gelfiltrationiscompatiblewithorganicandothersolventsthatdissolveorotherwisecompromisetheintegrityofdialysismembranes.Finally,incontrasttodialysis,gelfiltrationchromatographyallowsthecontaminatingmaterialtoberemovedinarelativelysmallvolume(andisleftonthecolumn),animportantfeaturewhenworkingwithtoxicorradioactivesubstances.LearnmoreOverviewofDialysis,Desalting,andBufferExchangeDialysisMethodsforProteinResearchProteinPreparationHandbookProteinPurificationandIsolationSupportCentereLearningCourse:ProteinIsolationandPurificationSelectproductsZebaDesaltingProductSelectionGuideProteinClean-upTechnicalHandbookLearnmoreaboutdesalting,bufferexchange,concentration,and/orremovalofcontaminantsfromproteinsamplesusingvariousThermoScientificproteinbiologytoolsinthis32-pagehandbook.DialyzeproteinsamplessecurelyusingSlide-A-LyzerdialysiscassettesanddevicesRapidlydesaltsampleswithhighproteinrecoveryusingZebaspindesaltingcolumnsandplatesEfficientlyextractspecificcontaminantsusingresinsoptimizedfordetergentorendotoxinremovalConcentratediluteproteinsamplesquicklyusingPierceproteinconcentratorsDownloadtheProteinClean-upTechnicalHandbook› Howgelfiltrationchromatographyworks Gelfiltrationseparatesmoleculesofdifferentdimensionsbasedontheirrelativeabilitiestopenetrateintoasuitablestationaryphaseorchromatographicresin.Theresinhassize-exclusionpropertiesandusuallyconsistsofverysmall,unchargedporousparticlesinanaqueoussolution,whicharepackedintoacolumnandthenusedfortheseparation.Theresinparticleshavearangeofporesizesthatdeterminethesizeofmoleculesthatcanbeseparated.Theaverageormaximumeffectiveporesizedefineswhatiscalledthefractionationrangeorexclusionlimitoftheresin.Moleculessmallerthanthefractionationrangecanentertheporesoftheresin,whilemoleculeslargerthanthefractionationrangeareexcludedfromenteringthepores.Whenasamplesolutionispassedthroughacolumnofpackedgelfiltrationresin,smallmoleculesinthesample(buffersalts,smallmolecules,etc.)entertheporesofresinbeadsthattheyencounterandareforcedtofollowacircuitouspathbeforelaterexitingthebeads.Bycontrast,largemoleculesflowaroundtheresinbeads,takingarelativelydirectpaththroughthecolumn.Ineffect,smallmoleculesexperienceamuchlargercolumnvolumethanlargemolecules.(Keepinmindthatresinbeadsareextremelyporous;mostoftheirtotalvolumeiswater).Thus,thedifferenceintheflowratesofsmallmoleculesandexcludedmoleculesallowsthefaster-flowingmacromoleculestobecomeseparatedfromtheslowersmallmoleculesasthesampletravelsthedistanceoftheresinbedpackedinthecolumn. Watchthisvideoonsampledesaltingusinggelfiltrationchromatography Whenanappropriategelfiltrationresinisused,manydifferentclassesofmacromoleculescanbeseparatedfrombuffersalts,unconjugatedlabelingreagentsandothermoleculestoachieverapidpurificationbeforedownstreamapplications.Thisisdonebypassingsamplesthroughacolumnwhoseresin-bedissufficientlytallandvoluminoustofullyseparatetheemergencefromtheendofthecolumnofmacromoleculescomparedtothesmallmolecules.Bycollectingsmallfractions,themacromoleculesareeasilyseparatedfromthesmallmoleculesemerginginthelaterfractions.Asmentionedabove,gelfiltrationcanbeeffectivelyutilizedforproteindesaltingandisaccomplishedbyfirstequilibratingthegelfiltrationcolumnwithwater.However,bufferexchangeisaccomplishedbyfirstequilibratingthecolumnresinwiththetargetbuffer.Inbothdesaltingandbuffer-exchangemodesofgelfiltration,thebufferconstituentscarryingthesampleintothecolumnwillbereplacedbythesolutioninwhichtheresinbedwasoriginallysaturated(i.e.,pre-equilibrated).Asaloadedsampleentersintoaresinbed,itdisplacesanidenticalvolumeofwaterorbufferalreadypresentinthecolumn.Assampleispushedthroughthecolumn(usuallybyadditionofmorebufferatthetopofthecolumn),theequilibrationsolutionispushedoutthroughtheendofthecolumn.Becausethemacromoleculesemergefromthecolumnbeforethebuffertheywereoriginallycarriedin,theyendupemergingfromthecolumnintheequilibrationsolution.Asdescribedinmoredetailinthesectionbelow,therearethreemethodsforperforminggelfiltrationthatemploytheuseofgravity-flowcolumns(dripcolumns),centrifuge(spin)columnsorchromatographycartridges.ThermoFisherScientifichasdevelopedvariousstrategiesforproteinsampledesalting.Forexample,ThermoScientificZebadesaltingspinplates,spincolumns,andcartridgescontainuniquegelfiltrationresinsandwerespecificallydesignedtoprovideconsistentperformanceoverawiderangeofproteinconcentrationsandsamplesizes.Highproteinrecoverycanbeachievedevenfordiluteproteinsamples.Comparisonofspindesaltingcolumns.ZebaSpinDesaltingColumns(7KMWCO,10mL)andDisposablePD-10DesaltingColumns(GEHealthcare)wereusedtodesalt1.5,2.5and3.5mLsamplesofbovineserumalbumin(BSA)atconcentrationsof0.04,0.2,and1mg/mL.Desaltingwasperformedaccordingtoeachmanufacturer’srecommendedprotocolsforeitherspin(centrifuge)ordrip(gravity)procedures.Threesetsofcolumnswereequilibratedinfinalbufferandthenloadedwith1.5,2.5,and3.5mLsamples.Foreachelectrophoresisgel,analiquotofstartingsampleequalto1µgofBSAwasloadedinLane1astheloadcontrol;allotherdesaltedsampleswereloadedinthegelatthesamevolumeastheloadcontrol.Differencesinintensitybetweenlanesareacombinationofproteinrecoveryandsampledilutioncausedbydesalting.ResultsofthisexperimentshowthatcomparedwithPD-10columns,the ThermoScientificZebaColumn provideshigherproteinrecoveryandlesssampledilutionoverawiderrangeofsampleconcentrationsandvolume. LearnmoreApplicationNote:BenchmarkingExperimentswithZebaSpinDesaltingColumnsSelectproductsZebaDesaltingProductSelectionGuide Methodsforgelfiltrationchromatography Thethreecommonformatsforperforminggelfiltrationincludegravity-flowcolumns,centrifugecolumnsorchromatographycartridges.Gravity-flow-ordrip-columnsandchromatographycartridgesusehead-pressurefromabuffer-chasetopushthesamplethroughagelfiltrationmatrix.Centrifugecolumnsusecentrifugalforcetomoveasamplethroughthematrix.Inthecaseofgravity-flowcolumns,sampleisloadedthroughthetopofanuprightcolumnandallowedtosinkintotheresinbed.Thesampleisthenchasedthroughthecolumnbyaddingadditionalbufferorwatertothetopofthecolumn.Duringthisprocess,smallfractionsarecollectedandeachistestedfortheproteinorothermacromoleculesofinterest.Insomecases,severalfractionsmightcontaintheproteinandmayhavetobepooledtoimproveyield.Chromatographycartridgesworkinmuchthesamewayasgravity-flowcolumnsexceptthatthesystemisclosedandliquidisforcedintothedevicewiththeaidoffluidpressuregeneratedfromasyringe-plunger,pumporotherdevice.ThermoScientificoffersavarietyofdesaltingcolumnsaswellaschromatographycartridgesforefficientsaltremovalandproteinrecovery.TheThermoScientificPierceZebaDesaltingChromatographyCartridges(7KMWCO,5mL)containtheZebaHigh-PerformanceResinfordesaltingorbufferexchangeapplications.Thisresinisidealforremovinglowmolecularweightcompoundsincludingsalts,fluorescentdyes,biotinandothersmalllabelingreagents.Proteinsamplescanbeprocessedwithahighdegreeofrecoveryand≥95%retentionofsaltsandothersmallmolecularcontaminants(<1,000Da).Efficientsaltremovalandproteinrecoveryusingdesaltingchromatographycartridge. Bovineserumalbumin(1mg)in1MNaClwasappliedto5mLThermoScientificPierceZebaCartridge(7KMWCO)ataflowrateof5mL/minute.CartridgeprofileshowsisocraticelutionofBSA(blue)andNaCldetectedbyconductivity(brown).Greaterthan95%oftheBSAwasrecoveredandmorethan95%ofthesaltwasremoved.       Parametersforgelfiltrationchromatography   Itisimportanttoselectacolumnsizethatissuitableforthevolumeofsampletobedesalted.Acolumnthatistoolargewillresultindilutionoftheproteinsample.Ifthecolumnistoosmall,thelowmolecularweightcontaminantswillnotbeadequatelyseparatedfromthemacromoleculeofinterest.Selectingacolumnsizeappropriateforthesamplevolumewillminimizedilutionandallowforcompleteandefficientseparation.Generally,acolumnwithabedvolumethatis4to20timeslargerthanthesamplevolumeisadequate.Thetypicallyexcludedvolume(i.e.,thecolumnvolumeavailabletolargemolecules)isabout35%oftheresinvolume,whilethetotalvolumeavailabletosmallmoleculesisnearlyequaltotheresin-bedvolume.Thesize-exclusionlimitofthegelfiltrationresinbedisalsoimportant.Fortypicaldesaltingandbufferexchangeapplications(asopposedtoothertypesofsize-exclusionchromatography),choosingaresinwithsize-exclusionlimits(MWCO)between2000and7000isusuallybest.Inpractice,thesmallmoleculesonewishestoremovemustbeseveraltimessmallerthantheMWCO;themacromolecules(e.g.,proteins)onewishestoseparatemustbeatleastaslargeastheMWCO.Forotherapplications,suchasseparatingpeptidesfromfull-sizedproteins,resinswithlargerexclusionlimits(e.g.,40K)maybenecessary.Beawarethatresinswithlargeexclusionlimitsarenotalwayssuitableforbufferexchangeanddesaltingbecausethesmallmoleculesflowalmostuninhibited(i.e.,withoutacircuitouspath)throughtheporesofthematrix.Commerciallyavailablegelfiltrationresinsaregenerallydurable,chemicallyresistantandinertandhaveminimalnonspecificbindingproperties.Consequently,nearlyanybuffersystemcanbeusedeffectivelyfordesaltingandbufferexchange.Whendesaltingproteinsintoawater-equilibratedcolumn,peak-broadeningcanresultcausingmoresampledilutionandpoorerseparationthanwhenabufferedsolutionisused.Generally,betterresultsareobtainedusingbufferedsolutionshavingsomeioniccharacter.Asanalternative,volatileelectrolytes(suchaspyridiniumacetate,ammoniumbicarbonateandethylenediamineacetate)canbeaddedtothedesaltingbuffertoincreasetheionicstrengthanddiminishthetailingeffectwhenseparationprecisioniscriticalforexperimentalsuccess.Theseadditivescanbeeasilyremovedlaterbylyophilization.   Watchthisvideotolearnmoreaboutdesaltingcolumns   DropVideoDropPlayer(overridesdefault)           LearnmoreTechTip#40: Convertbetweentimesgravity(xg)andcentrifugerotorspeed(RPM)TechTip#29: DegasbuffersforuseinaffinityandgelfiltrationcolumnsApplicationNote: ChromatographyCartridgesforDesaltingandAffinityPurificationProteinPreparationHandbookeLearningCourse: ProteinIsolationandPurification       SelectproductsDesaltingColumnsSpinCupsandColumnsCentrifugeColumnsDesaltingColumnsEmptySpinandGravity-flowChromatographyColumns                 Recommendedreading   Porath,J.andFlodin,P.(1959(Gelfiltration:amethodfordesaltingandgroupseparation.Nature183:1657-1659.WalkerJM.2009.TheProteinProtocolsHandbook.ThirdEdition.Springer-VerlagNewYork,LLC.             ForResearchUseOnly.Notforuseindiagnosticprocedures.           Edit              Edit          BreadCrumb      Edit               Edit          Divider      Cut        Copy        Paste        Delete               Startof2Columns      Edit         Delete        New...        Paste          EndofColumns       Divider      Cut        Copy        Paste        Delete               Well      Edit        Annotate         Cut        Copy        Paste         New...        Paste        Delete              Well      Edit        Annotate         Cut        Copy        Paste         New...        Paste        Delete              Divider      Cut        Copy        Paste        Delete               Divider      Cut        Copy        Paste        Delete               Divider      Cut        Copy        Paste        Delete               Divider      Cut        Copy        Paste        Delete               Well      Edit        Annotate         Cut        Copy        Paste         New...        Paste        Delete              Divider      Cut        Copy        Paste        Delete               InheritedParagraphs       InheritedParagraphs       InheritedParagraphs       Startof2Columns      Edit         Delete        New...        Paste          Startof2Columns      Edit         Delete        New...        Paste          EndofColumns       EndofColumns       Startof2Columns      Edit         Delete        New...        Paste          EndofColumns                                 mallika.pathania(thisweek)       ColumnParsys:DragcomponentsorassetshereColumnParsys:DragcomponentsorassetshereMainParsys:DragcomponentsorassetshereColumnParsys:DragcomponentsorassetshereColumnParsys:DragcomponentsorassetshereColumnParsys:DragcomponentsorassetshereColumnParsys:Dragcomponentsorassetshereuipar:Dragcomponentsorassetshereuipar:Dragcomponentsorassetshereuipar:DragcomponentsorassetshereColumnParsys:DragcomponentsorassetshereColumnParsys:DragcomponentsorassetshereheaderParsys:Dragcomponentsorassetshere Componentsdroppedherewillappearonlyonthispage railParsys:DragcomponentsorassetsherebannerParsys:Dragcomponentsorassetshere ThinBannercomponentistheonlycomponentallowedinthiscontainer.Itwillbeinheritedtoallchildren. MainInheritParsys:Dragcomponentsorassetshere RawHTMLcomponentandreferencecomponentsaretheonlycomponentsallowedinthiscontainer.Itwillbeinheritedtoallchildren. railInheritParsys:Dragcomponentsorassetshere                                                                  Efficientsaltremovalandproteinrecoveryusingdesaltingchromatographycartridge. Bovineserumalbumin(1mg)in1MNaClwasappliedto5mLThermoScientificPierceZebaCartridge(7KMWCO)ataflowrateof5mL/minute.CartridgeprofileshowsisocraticelutionofBSA(blue)andNaCldetectedbyconductivity(brown).Greaterthan95%oftheBSAwasrecoveredandmorethan95%ofthesaltwasremoved. Centrifuge-orspin-columnsareuniqueinthattheforcegeneratedbyacentrifugeissufficienttopushthesamplethroughtheresinbedwithoutanybuffer-chase.Thecentrifugalforcecausesthegelmatrixtocollapsetosomeextent,helpingtosqueezethesamplethroughandoutthebottomofthecolumnandtotrapsmallmoleculesthatentertheporesoftheresinbeads.Spindesaltingisnotonlyfasterthangravity-flowandcartridgeformats,italsoreducestheamountofsampledilution. Parametersforgelfiltrationchromatography Itisimportanttoselectacolumnsizethatissuitableforthevolumeofsampletobedesalted.Acolumnthatistoolargewillresultindilutionoftheproteinsample.Ifthecolumnistoosmall,thelowmolecularweightcontaminantswillnotbeadequatelyseparatedfromthemacromoleculeofinterest.Selectingacolumnsizeappropriateforthesamplevolumewillminimizedilutionandallowforcompleteandefficientseparation.Generally,acolumnwithabedvolumethatis4to20timeslargerthanthesamplevolumeisadequate.Thetypicallyexcludedvolume(i.e.,thecolumnvolumeavailabletolargemolecules)isabout35%oftheresinvolume,whilethetotalvolumeavailabletosmallmoleculesisnearlyequaltotheresin-bedvolume.Thesize-exclusionlimitofthegelfiltrationresinbedisalsoimportant.Fortypicaldesaltingandbufferexchangeapplications(asopposedtoothertypesofsize-exclusionchromatography),choosingaresinwithsize-exclusionlimits(MWCO)between2000and7000isusuallybest.Inpractice,thesmallmoleculesonewishestoremovemustbeseveraltimessmallerthantheMWCO;themacromolecules(e.g.,proteins)onewishestoseparatemustbeatleastaslargeastheMWCO.Forotherapplications,suchasseparatingpeptidesfromfull-sizedproteins,resinswithlargerexclusionlimits(e.g.,40K)maybenecessary.Beawarethatresinswithlargeexclusionlimitsarenotalwayssuitableforbufferexchangeanddesaltingbecausethesmallmoleculesflowalmostuninhibited(i.e.,withoutacircuitouspath)throughtheporesofthematrix.Commerciallyavailablegelfiltrationresinsaregenerallydurable,chemicallyresistantandinertandhaveminimalnonspecificbindingproperties.Consequently,nearlyanybuffersystemcanbeusedeffectivelyfordesaltingandbufferexchange.Whendesaltingproteinsintoawater-equilibratedcolumn,peak-broadeningcanresultcausingmoresampledilutionandpoorerseparationthanwhenabufferedsolutionisused.Generally,betterresultsareobtainedusingbufferedsolutionshavingsomeioniccharacter.Asanalternative,volatileelectrolytes(suchaspyridiniumacetate,ammoniumbicarbonateandethylenediamineacetate)canbeaddedtothedesaltingbuffertoincreasetheionicstrengthanddiminishthetailingeffectwhenseparationprecisioniscriticalforexperimentalsuccess.Theseadditivescanbeeasilyremovedlaterbylyophilization. Watchthisvideotolearnmoreaboutdesaltingcolumns xLearnmoreTechTip#40:Convertbetweentimesgravity(xg)andcentrifugerotorspeed(RPM)TechTip#29:DegasbuffersforuseinaffinityandgelfiltrationcolumnsApplicationNote:ChromatographyCartridgesforDesaltingandAffinityPurificationProteinPreparationHandbookeLearningCourse:ProteinIsolationandPurificationSelectproductsDesaltingColumnsSpinCupsandColumnsCentrifugeColumnsDesaltingColumnsEmptySpinandGravity-flowChromatographyColumns Recommendedreading Porath,J.andFlodin,P.(1959(Gelfiltration:amethodfordesaltingandgroupseparation.Nature183:1657-1659.WalkerJM.2009.TheProteinProtocolsHandbook.ThirdEdition.Springer-VerlagNewYork,LLC.ForResearchUseOnly.Notforuseindiagnosticprocedures. Signin Don'thaveanaccount? 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