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胶原蛋白、纤连蛋白、玻连蛋白、水性凝胶、低代成纤维细胞
℡ 4000-520-616
℡ 4000-520-616
Advanced BioMatrix/PureCol®//5005-1000ML
产品编号:5005-1000ML
市  场 价:¥67000.00
场      地:美国(厂家直采)
联系QQ:1570468124
电话号码:4000-520-616
邮      箱: info@ebiomall.com
美  元  价:$3350.00
品      牌: Advanced BioMatrix
公      司:Advanced BioMatrix ,Inc.
公司分类:
Advanced BioMatrix/PureCol®//5005-1000ML
商品介绍

ProductDescription

PureCol®collagenisknownasthestandardofallcollagensforpurity(>99.9%collagencontent),functionality,andthemostnative-likecollagenavailable.PureCol®isisolatedfrombovinehidessourcedfromtheonlycontrolled,closedherdintheUnitedStates.AdvancedBiomatrix’smanufacturingprocessescomplywithstringentqualitystandardsthathaveproventoyieldunsurpassedlot-to-lotconsistency.

PureCol®collagenisapproximately97%TypeIatelocollagenwiththeremainderbeingcomprisedofTypeIIIcollagen.PureCol®collagenissuppliedatapproximatelya3mg/mlconcentration.TheconcentrationforeachspecificlotisprovidedonaCertificateofAnalysisthatisavailablewiththepurchaseofeachproduct.PureCol®issolubleatelocollagenin0.01NHCI,therefore,thepHis2.PureCol®collagenisidealforcoatingofsurfaces,providingpreparationofthinlayersforculturingcells,oruseasasolidgel.

PureCol®collagenisprovidedinauser-friendlypackagingforuseandstorage.PureCol®issterilefilteredandissuppliedasareadytousesolution.

Parameter,Testing,andMethodPureCol®TypeICollagen#5005
SterilizationMethodFiltration
ExtractionMethodEnzyme-atelocollagen
FormSolution
PackageSize100mL,1000mL
StorageTemperature2-10°C
ShelfLifeMinimumof6monthsfromdateofreceipt

CollagenConcentration-Biuret

2.9-3.2mg/mL

CollagenPurity-SilverStaining

>99.9%
pH1.9-2.1
KineticGelTest(Minutes)<40
GelFormationTubeTest(Minutes)<40

Fibrillogenesis(AbsorbanceUnits)

>0.5

ElectrophoreticPattern-CoomassieBlue

Characteristic
Sterility-USPmodifiedNogrowth
Endotoxin-LAL<1.0EU/mL
Osmolality(mOsmoH2O/kg)<35
CellAttachmentAssayPass
SourceBovineHide
HydrogelYoung"sModulusE(Pa)Characteristic

DirectionsforUse

DownloadthefullPDFversionorcontinuereADIngbelow:

CoatingProcedure

Note:Usetheserecommendationsasguidelinestodeterminetheoptimalcoatingconditionsforyourculturesystem.

  1. Removerequiredquantityofcollagenfromthebottleanddispenseintoadilutionvessel.
  2. DilutePureCol®inwaterto~50to100µg/ml(~1:30).A0.01NHClsolutionmayalsobeused.
  3. Swirlcontentsgentlyuntilmaterialiscompletelymixed.
  4. AddappropriateamountofdilutedPureCol®materialtotheculturesurfaceensuringthattheentiresurfaceiscoated.
  5. Incubateatroomtemperature,covered,for1-2hours.Aspirateanyremainingmaterial.Alternatively,incubateatroomtemperatureuntilsurfaceisdry.
  6. RinsecoatedsurfacescarefullywithsterilemediumorPBS,avoidscratchingsurfaces.
  7. Coatedsurfacesarereadyforuse.Theymayalsobestoredat2-10°Cdamporairdriedifsterilityismaintained.

3-DGelPreparationProcedure

  1. Slowlyadd1partofchilled10XPBSor10Xculturemediato8partsofchilledcollagensolutionwithgentleswirling.
  2. AdjustpHofmixtureto7.0–7.5usingsterile0.1MNaOH.MonitorpHadjustmentcarefully(pHmeter,phenolred,orpHpaper).
  3. Adjustfinalvolumetoatotalof10partswithsterilewater.
  4. Topreventgelation,maintaintemperatureofmixtureat2–10°C.
  5. Toformgel,warmto37°C.Allowapproximately90to120minutesforgelformation.

ProductQ&A

ThepurityofPureCol®collagenisdeterminedbySDS-PAGE,sodiumdodecylsulfatepolyacrylamidegelelectrophoresisinconjunctionwithbacterialCollagenasesensitivityandsilverstainingtechniqueswithamethodsensitivityof99.9%.ItwasfoundthatPureCol®collagenis95to98%TypeIcollagenandtheremainderbeingcomprisedofTypeIIIcollagen.

SDSpolyacrylamidegelelectrophoresisdemonstratesthepresenceofalpha,betaandgammacomponentsinanappropriateratioofapproximately40:30:30,respectively.PureCol®collagenisanativecollagenasjudgedbypolarimetryandtrypsinsensitivityalthoughtheproductdoescontainalowpercentageofcollagenfragmentsorshortenedhelices.

Conclusion:Withthetestmethodsensitivityof99.9%(SDS-PAGEgelelectrophoresisinconjunctionwithbacterialcollagenasesensitivityandsilverstainingtechniques)andnootherproteinspresentinthepreparation,itcanbeconcludedthatthepurityofthePureCol®collagenis99.9%.

TheviscosityofPureCol®is~32cp.

PureCol®producthasanisoelectriczoneinsteadofisoelectricpoint.TheisoelectriczoneispH7to8.Inaddition,thecollagenmoleculesinthePureCol®productwillcomeoutofsolutionstartingatapHabove5.5andreachitsplateauatpH7to8thengraduallytaperingoffatpH8to9.5.

Reductionofacommerciallyavailable,pepsin-solubilized,bovinedermalcollagen(Vitrogen100)(PureCol’soldproductname)withsodium[3H]borohydrideprovidedradiolabeledcollagenpreparationswithspecificactivitiesrangingfrom7.1-12.0muCi/mgcollagen.Thesespecificactivitieswere2-3timesgreaterthanthoseobtainedbyreductionofintactrattailtendoncollagenundersimilarconditions.

Thealpha,beta,andhigheraggregatecomponentsoftypeIcollagenwereradiolabeledaswellasthealphacomponentofasmallamountoftypeIIIcollagenpresentinthesamples.Fractionationofcyanogenbromidepeptidesshowedthatalpha1(I)CB7,alpha1(I)CB8,andalpha2(I)CB3,5werethepredominantpeptideslabeledbythisprocedure.AminoacidanalysisindicatedthatthemajorityoftheradioactivitywasinreducIBLecross-links,precursorsofthesecross-links,andinhexosyllysineresidues.

Reconstitutionexperimentscomparingthisradiolabeledcollagenwithnonlabeledcollagenshowedthemtobeindistinguishable.Bacterialcollagenasedigestionofthisreconstitutedfibrillarcollageninbothalightlycross-linked(glutaraldehyde0.0075%)andnoncross-linkedformprovidedevidencethatdigestionoflabeledandnonlabeledcollagensproceededatsimilarrates.Thus,labelingdidnotchangethepropertiesofthecollagen.Cross-linkingmadethepreparationrefractorytoproteolyticdegradation.Injectionoffibrillarcollagenpreparations,spikedwithradiolabeledcollagen,intotheguineapigdermisfollowedbyquantitationoftheamountofradioactivityrecoveredfromimplantsitesasafunctionoftime,indicatedthatthelightlycross-linkedsamplesalsoweremoreresistanttodegradationinvivothanthenoncross-linkedpreparation.

Thehalf-lifeofnoncross-linkedcollagenwasabout4dayswhilethatofthecross-linkedcollagenwasabout25days.Thesedegradationratesweremuchfasterthanobservedforsimilar,nonlabeledsamplesinjectedintothedermisofhumans,presumablyduetoahighermetabolicactivityintheguineapigdermis.

SincethecollageninPureColcollagencontainsapproximately95%TypeIbovinecollagenand5%TypeIIIbovinecollagen,ananti-bovinecollagenTypeIantibodyforyourstudycanbeused.

Thereisnodifference.Vitrogenwastheoldtradename,andPureCol®isthenewtradename.

WecompletedastudytoshowthatDNAiscompletelydestroyedatpH2,anddemonstratedthatourcollagenproductsdonotcontainDNA.

Thecollagenisfullyhydrolyzed.TheaminoacidanalysisisdoneusingtheWatersAccQ-Tagderivatizationmethod.Duringtheacidhydrolysisstep,asparagine(N)isconvertedtoasparticacid(D)andglutamine(Q)isconvertedtoglutamicacid(E).Tryptophan(W),ifpresent,isdestroyedduringacidhydrolysis.Experimentally,onecandeterminethepicomoles(pmol)ofeachaminoacidperinjecteddetectedusingaminoacidstandards.Fortheconcentrationdetermination,thetotalnumberofpmolofeachaminoacidissummedtogetthetotalpmolofthe18aminoacidsdetected.Thetotalpmolaminoacidsisdividedbythetheoreticalnumberofaminoacidresiduesincollagenbasedonthepublishedsequence.Theresultisthepmolofcollageninjected.Theresultisthenmultipliedbythedilutionand300,000isusedasthecollagenmolecularweighttogettomg/mL.Themolecularweightofcollagenisnotwellagreedupon.

Dilutingwith1XPBS(ratherthanwateror0.01NHCl)wouldhaveaneffectforcoatingpurposes.ItwouldchangethepHofthedilutedcollagensolutionfromacidtoneutralpH.ThepHchangewilltransformthecollagenmoleculesfromamolecularformtoafibrillarform;andthenthenatureofcoatingsurfacewillbechangedfromamonomericcoatingtoafibrillarcoating.

WeusethefollowingantibodiesfromSouthernBiotech:

1.1310-02–GoatAnti-TypeICollagen-FITC

2.1310-08–GoatAnti-TypeICollagen-BIOT

3.7100-05–Streptavidin-HRP

ThemajorcollagenmolecularspeciesinourTypeIcollagenproductsaremonomers(approx.70%),buttherearedimers,trimersandafewpercentagesofoligomerstoo(approx.30%)withsomeminoramountsofcollagenfragments.Thecollagenmonomerisarodshapedmoleculewith300nminlengthand1.5nmindiameter.Thedimer,trimerandoligomerare600nm,900nmandevenlongerinlengthrespectively.Accordingtothecoatingprocedures,thecollagenmoleculesareattachedtothechargedpolystyrenesurfacerandomlybychargeoraffinityinacidconditionsduringthe1-2hrsincubationperiodat37°C,andanyunattachedmaterialsareremovedbyaspirationandrinsing.Therefore,thecoatedsurfaceisasinglelayerofcollagenmonomer,dimer,trimerandoligomermixtures.Thethicknessofthemono-molecularlayerisdependentonhowthosemoleculesareattachedonthesurface.Thecoatingdensitythicknesswouldgenerallybecharacterizedasa1moleculethicknesswhichcouldberangingfromafewnanometerstoafewhundrednanometerswiththewholesurfacebeingcoveredbycollagen.

ThenetchargeofTypeIcollagenproducts’(PureCol®,BovineCollagenandVitroCol®,HumanCollagen)moleculeisdirectlyrelatedtothepH.AtanacidicpH,theaminoacids(zwitterions)alongthecollagenmoleculearepositivelycharged,makingtheentirecollagenmoleculepositive.Attheisoelectricpoint(orzone)ofcollagen,aroundpH7-8,theaminoacidsalongthecollagenmoleculearepositivelyandnegativelycharged,makingthenetchargeofthecollagenmoleculeclosetozero.AtabasicpH,theaminoacidsalongthecollagenmoleculewerenegativelycharged,makingtheentirecollagenmoleculenegative.

Further,thenatureofthechargeofthecollagencoatingsurfacewillbedependentonthetypeofcoatingapplied.ForamonomericcollagencoatingswhenthecollagenisappliedunderanacidicpHcondition,thesurfaceispositivelycharged.IfthesurfaceisrinsedwithpHneutralbufferormediathenitwillchangethechargeofthecollagensurfacenetchargeclosetozero.Fora3Dgelcoating,thecollagenpreparedunderneutralpH;thenetchargeofthecollagensurfaceisclosetozero.

Usingrotaryshadowingtechniqueundertransmissionelectronmicroscopy,itwasfoundthatourcollagen,onaverage,consistsofapproximately80%monomers,13%dimers,trimers,andoligomerswiththeremaining7%collagenfragments.

Yes.ThecollagenmoleculeinPureCol,Nutragen,VitroCol,andallofourotherAtelocollagenproductswerepreparedfromnativecollagenmatrixbypepsintreatmentundercontrolledconditionstoremovethenon-helicalportion,telo-peptides,onlyandthehelicalportionisintact.Inthiscase,theenzymaticactivesitesforMMP(MatrixMetalloproteinase),suchasforMammalianCollagenaseMatrixMetalloproteinase8(MMP-8),onthemoleculewaspreserved.

Thesepepsintreatedcollagenproductsshouldbehaveasnativeintactcollagen.

TGFbetawouldhavebeendigestedwiththepepsinenzymaticdigestionstep.ItwasundetectablebySDSPAGEsilverstainaswell.Wedidn’tdoanyspecificmeasurementsbyELISAhoweverbutpresencesofTGFbetaisnotanticipated.

WeprimarilyusetheBiuretmethod,butwealsouseBCA,AAA,andhydroxyl-prolineassays.

-Collagensolutionsthatarefrozentendtohaveissuesforming3Dhydrogels,andwilllikelynotwork.Thesolutionsshouldstillbegoodfor2Dcoatings.

-Collagensolutionsthatareleftoutatroomtemperatureforextendedperiodsoftimemayshowsignsofdegradation,whichwillaffecttheformationof3Dhydrogels.Itislikelystillfinefor2Dcoatings.

Ourrecommendationisthis:Ifyouareusingtheproductdirectlyforapublication,wehighlysuggestbuyinganewbottleiftheoneyouhavewascompromised.

ProductReferences

BecausePureCol®hasbeencitedinover2000publications,wehaveonlypostedafewbelow:

Sorensen,JacobR.,etal."Analteredresponseinmacrophagephenotypefollowingdamageinagedhumanskeletalmuscle:implicationsforskeletalmusclerepair."TheFASEBJournal(2019):fj-201900519R.

Sorensen,JacobR.,etal."Analteredresponseinmacrophagephenotypefollowingdamageinagedhumanskeletalmuscle:implicationsforskeletalmusclerepair."TheFASEBJournal(2019):fj-201900519R.

Colaço,E.,etal."HierarchicalCollagen-HydroxyapatiteNanostructuresDesignedThroughLayer-by-LayerAssemblyofCrystal-DecoratedFibrils."J.,HierarchicalCollagen-HydroxyapatiteNanostructuresDesignedThroughLayer-by-LayerAssemblyofCrystal-DecoratedFibrils(May13,2019)(2019).

Schwerdtfeger,LukeA.,etal."Humancolonfunctionexvivo:Dependenceonoxygenandsensitivitytoantibiotic."PloSone14.5(2019):e0217170.

Cardoso,Ana,etal."MiR-144overexpressionasapromisingtherapeuticstrategytoovercomeglioblastomacellinvasivenessandresistancetochemotherapy."Humanmoleculargenetics(2019).

Steele,HannahE.,etal."MechanotransductionofmitochondrialAMPKanditsdistinctroleinflow-inducedbreastcancercellmigration."Biochemicalandbiophysicalresearchcommunications514.2(2019):524-529.

Gehwolf,Renate,etal."GlobalResponsesofIl-1β-Primed3DTendonConstructstoTreatmentwithPulsedElectromagneticFields."Cells8.5(2019):399.

Alexander,Frank,SebastianEggert,andDoriellePrice."Label-FreeMonitoringof3DTissueModelsviaElectricalImpedanceSpectroscopy."(2019):1-24.

Matysik-Woźniak,Anna,etal."ExaminationofKynurenineToxicityonCornealandConjunctivalEpithelium:InvitroandinvivoStudies."Ophthalmicresearch(2019):1-12.

Compton,Clayton,etal."ReconstitutionoftheVentricularEndocardiumWithinAcellularHearts."RegenerativeEngineeringandTranslationalMedicine(2019):1-11.

Müller,A.L.,etal."4.IdentificationofmiR-301ainPrimaryHumanAtrialFibroblastsandBoneMarrow-DerivedMesenchymalProgenitorCellstoAttenuateEndogenousDifferentiationintoPro-FibroticCells."DifferentiationofPrimaryHumanPro-FibroticMesenchymalCellsInfluencedbyExtracellularMatrixEnvironmentDeterminedbyMicro-RNAExpression(2018):130.

Doblinger,Nina,etal."Impactofhydroxyethylstarchandmodifiedfluidgelatinongranulocytephenotypeandfunction."Transfusion(2019).

Elisabeth,etal."Pro-InflammatoryResponsesinHumanBronchialEpithelialCellsInducedbySporesandHyphalFragmentsofCommonDampIndoorMolds."Internationaljournalofenvironmentalresearchandpublichealth16.6(2019):1085.

Dodmane,PuttappaR.,etal."BiphasicchangesinairwayepithelialcellEGFreceptorbindingandphosphorylationinducedbycomponentsofhogbarndust."Experimentallungresearch44.10(2018):443-454.

McClellan,Alyce,etal."Anovelmechanismfortheprotectionofembryonicstemcellderivedtenocytesfrominflammatorycytokineinterleukin1beta."Scientificreports9(2019).

Wang,Weiling,etal."Aquaporin-3deficiencyslowscystenlargementinexperimentalmousemodelsofautosomaldominantpolycystickidneydisease."TheFASEBJournal(2019):fj-201801338RRR.

Teo,JyeYng,etal."SurfacetetheringofstemcellswithH2O2-responsiveanti-oxidizingcolloidalparticlesforprotectionagainstoxidation-induceddeath."Biomaterials201(2019):1-15.

Gehwolf,Renate,etal."3D-EmbeddedCellCulturestoStudyTendonBIOLOGy."(2019):1-11.

ProductCertificateofAnalysis

Noresultfor.

ProductVideos

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SafetyandDocumentation

SafetyDataSheet

CertificateofOrigin

DeclarationofMaterialSource

ProductDisclaimer

ThisproductisforR&Duseonlyandisnotintendedforhumanorotheruses.PleaseconsulttheMaterialSafetyDataSheetforinformationregardinghazardsandsafehandlingpractices.

品牌介绍
美国Advanced BioMatrix(简称ABM) www.advancedbiomatrix.com
Advanced BioMatrix(简称ABM)是美国一家著名的生物公司,获得了Allergan Inc的授权(Allergan用25年时间不断完善胶原蛋白相关的产品的生产工艺),将Allergan的专业和技术用于蛋白生产与检测,致力于为组织工程、细胞分析及细胞增殖等研究领域提供优质稳定的产品。

Advanced BioMatrix不断丰富已有产品线,目前可为三维细胞培养提供各种胶原蛋白、纤连蛋白、玻连蛋白、水性凝胶、不同粘度与分子量的透明质酸以及低代成纤维细胞等。在美国全部产品授权Sigma销售。

Advanced BioMatrix是组织培养,细胞分析和细胞增殖三维(3D)应用的生命科学领域的领导者。 我们的产品被公认为纯度,功能性和一致性的标准。
我们在生产,分离,纯化,冷冻干燥,细胞培养和蛋白质测试,粘附肽,附着因子,底物刚性和其他3D矩阵产品方面拥有丰富的专业知识。 我们的专业技术和知识正在被用来确保我们的产品质量最高,批次之间一致且易于为我们的研究客户使用。

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