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NEB/Protein Deglycosylation Mix II/P6044S/20 reactions

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貨號: P6044S-20reactions

品牌: NEB

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詳情
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常見問題

- Description:
  Glycosylationisoneofthemostcommonpost-translationalmodificationsofproteins,asshowninFigure1.N-linkedglycosylationoccurswhenglycansareattachedtoasparagineresiduesonthecoreprotein.O-linkedglycosylationoccurswhenglycansareattachedtoserineorthreonineresidues.Bothchemicalandenzymaticmethodsexistforremovingoligosaccharidesfromglycoproteins.However,chemicalmethodssuchasβ-eliminationwithmildalkaliormildhydrazinolysiscanbeharshandmayresultinincompletesugarremovalanddegradationoftheprotein;whereas,enzymaticmethodsaremuchgentlerandcanprovidecompletesugarremovalwithnoproteindegradation.
  
  PNGaseFisthemosteffectiveenzymaticmethodforremovingalmostallN-linkedoligosaccharidesfromglycoproteins.PNGaseFdigestiondeaminatestheaspargineresiduetoasparticacid,andleavestheoligosaccharideintact,keepingitsuitableforfurtheranalysis.Oligosaccharidescontainingafucoseα(1-3)-linkedtotheglycancoreare,however,resistanttoPNGaseFwhichcanoccuronsomeplantandinsectglycoproteins.
  
  ToremoveO-linkedglycans,monosaccharidesmustberemovedbyaseriesofexoglycosidasesuntilonlytheGalβ1-3GalNAc(core1)and/ortheGlcNAcβ1-3GalNAc(core3)coresremainattachedtotheserineorthreonine.NEB’sO-Glycosidase,clonedfromEnterococcusfaecalis,canthenremovethesecorestructureswithnomodificationoftheserineorthreonineresidues.Anymodificationofthecorestructures,includingsialyation,willblocktheactionoftheO-Glycosidase.Sialicacidresiduesareeasilyremovedbyageneralα2-3,6,8,9NeuraminidaseA.Inaddition,exoglycosidasessuchasβ(1-4)GalactosidaseSandβ-N-Acetylhexosaminidase_fcanbeincludedindeglycosylationreactionstoremoveothercomplexmodificationsoftenknowntobepresentonthecorestructures.ThiscombinationofenzymesmaynotremoveallO-linkedoligosaccharidesbutshouldremovemanycommonoligosaccharidestructures.
  
  TheProteinDeglycosylationMixIIcontainsalloftheenzymes,reagents,andcontrolsneededtoremoveallN-linkedandsimpleO-linkedglycansaswellassomecomplexO-linkedglycans.Thismixcontainsenzymesufficientfor20reactionsorthecleavageofasmuchas2mgofglycoprotein.AlloftheenzymesandreagentsincludedintheProteinDeglycosyationMixIIareMassSpectrometrycompatIBLe.Followingthedeglycosylationreaction,samplesarereadytobepreparedformassspectrometryanalysis.
  
  Figure1:AGlycoproteinmodifiedwithO-linkedandN-linkedglycosylation.
  
  Figure2
  
  EnzymaticDeglycosylationofBovineFetuinunderbothnative(10XDeglycosylationMixBuffer1)andreducing(10XDeglycosylationMixBuffer2)conditions.20μgreactionswereloadedontoa10-20%Tris-glycineSDS-PAGEgel.
  Lane1:???ColorPrestainedProteinStandard,BroadRange(11-245?kDa)(NEB#P7712)
  Lane2:???20?μguntreatedFetuincontrol
  Lane3:???20μgFetuindeglycosylatedundernativeconditionswithDeglycosylationMixBuffer1
  Lane4:???20μgFetuindeglycosylatedunderreducingconditionswithDeglycosylationMixBuffer2
  Lane5:???5μlProteinDeglycosylationMixII.
  
  ProteinDeglycosylationMixII:
  PNGaseF(Glycerol-free),Recombinant:
  10,000units/vial
  
  O-Glycosidase:
  80,000units/vial
  
  α2-3,6,8,9NeuraminidaseA:
  400units/vial
  
  β1-4GalactosidaseS:
  960units/vial
  
  β-N-acetylhexosaminidase_f:
  300units/vial
  
  SubstrateControl:
  Fetuin,0.5mg(FetuincontainssialylatedN-linkedandO-linkedglycans)
  
  ofEnzymesIncludedintheProteinDeglycosylationMixII
  O-Glycosidase(NEB#P0733),alsoknownasEndo-α-N-Acetylgalactosaminidase,isarecombinantenzymeclonedfromEnterococcusfaecalis(1).Itcatalyzestheremovalofcore1andcore3O-linkeddisaccharidesfromglycoproteins.Themolecularweightisapproximately147kDa.
  
  PNGaseF(Glycerol-free),Recombinant(NEB#P0709),alsoknownasPeptide:N-glycosidaseF,isclonedfromElizabethkingiamiricola(formerlyFlavobacteriummeningosepticum)andexpressedinE.coli(2).PNGaseF(Glycerol-free),RecombinantisanamidasewhichcleavesbetweentheinnermostGlcNAcandasparagineresiduesofhighmannose,hybrid,andcomplexoligosaccharidesfromN-linkedglycoproteinsunlessα(1-3)corefucosylated.Themolecularweightisapproximately36kDa.
  
  α2-3,6,8,9NeuraminidaseA(NEB#P0722),alsoknownasSialidaseA,isarecombinantenzymeclonedfromArthrobacterureafaciensandexpressedinE.coli(3).Itcatalyzesthehydrolysisofα2,3,α2,6,α2,8andα2,9linkedN-acetylneuraminicacidresiduesfromglycoproteinsandoligosaccharides.Themolecularweightisapproximately100kDa.
  
  β1-4GalactosidaseS(NEB#P0745),isarecombinantenzymeclonedfromStreptococcuspneumoniaeandexpressedinE.coli(4).Itisahighlyspecificexoglycosidasethatcatalyzesthehydrolysisofβ1-4linkedgalactoseresiduesfromoligosaccharides.Themolecularweightisapproximately231kDa.
  
  β-N-Acetylhexosaminidase_f(NEB#P0721),isarecombinantenzymeclonedfromStreptomycesplicatus(5)andoverexpressedinE.coli(6).Itcatalyzesthehydrolysisofterminalβ-N-acetylgalactosamineandglucosamineresiduesfromoligosaccharides.Themolecularweightisapproximately100kDa.
  ReagentsSupplied
  Thefollowingreagentsaresuppliedwiththisproduct:
  Storeat(°C) Concentration
  DeglycosylationMixBuffer1 -20 10X
  DeglycosylationMixBuffer2 -20 10X
  Notes:
  TheProteinDeglycosylationMixIIissuppliedwithtwodifferentreactionbuffers.Pleasereferencethe“ProtocolsandManuals”tabforthespecificprotocolassociatedwitheachbuffersystem.The10XDeglycosylationMixBuffer1(NEB#B6044)shouldbeusedwhennative(non-denaturing)conditionsarenecessary.The10XDeglycosylationMixBuffer2(NEB#B6045)willreducetheglycoprotein,butwillalsoprovidethemostefficientandcompletelevelofdeglycosylation.Ifnon-denaturingconditionsarenotrequired,werecommendusing10XDeglycosylationMixBuffer2.Storage:Itisrecommendedtostorethiskitat4°C.Allcomponentsofthekitwillbestableforatleastoneyearifstoredcorrectly.TheProteinDeglycosylationMixIIisnotrecommendedforuseonMucin-likesubstrates.
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NEB/Protein Deglycosylation Mix II/P6044S/20 reactions

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ReagentsSupplied

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	Storeat(°C)	Concentration
DeglycosylationMixBuffer1	-20	10X
DeglycosylationMixBuffer2	-20	10X