Formulation	50%glycerol/water(v/v)
Storage	-20°C
Purity	>95%bySDS-PAGE
ActivityDetermination	Clottingassay
ShelfLife(properlystored)	12months

DomainStructureofFactorX
ThedomainstructureoffactorXisrepresented,where:GLA=regioncontainingγ-carboxyglutamicacidresidues,EGF=regioncontainingsequenceshomologoustohumanepidermalgrowthfactor,AP=activationpeptidereleaseduponconversionofthezymogentotheactiveserineprotease,CATALYTICDOMAIN=regioncontainingtheserineproteasecatalytictriad.ThearrowindicatesthesitewhichisproteolyticallycleavedbyfactorXaseduringactivationofthezymogen.

SampleGelInformation:

Gel	Novex4-12%Bis-Tris
Load	HumanFactorX,1µgperlane
Buffer	MOPS
Standard	SeeBluePlus2;Myosin(191kDa),PhosphorylaseB(97kDa),BSA(64kDa),GlutamicDehydrogenase(51kDa),AlcoholDehydrogenase(39kDa),CarbonicAnhydrase(28kDa),MyoglobinRed(19kDa),Lysozyme(14kDa)

Overview:

FactorXisavitaminK-dependentproteinzymogenwhichissynthesizedintheliverandcirculatesinplasmaasatwochainmoleculelinkedbyadisulfidebond(1,2).Priortosecretionintoplasma,post-translationalmodificationsproduce11gamma-carboxyglutamicacid(gla)residuesandasingleb-hydroxyasparticacidresidue,whicharelocatedwithintheNH2-terminallightchain.Thelightchainalsocontainstwoepidermalgrowthfactor(EGF)homologydomains.TheCOOH-terminalheavychainoffactorXcontainsmostofthecarbohydratemoieties,aswellasthelatentserineproteasedomain.TheactivationoffactorXiscatalyzedbyeithertheintrinsicfactorXasecomplex(factorIXa,factorVIIIa,cellularsurfaceandcalciumions)ortheextrinsicfactorXasecomplex(factorVIIa,tissuefactor,cellularsurfaceandcalciumions).ActivationofhumanfactorXbyeithercomplexresultsincleavageatArg52-Ile53oftheCOOH-terminalheavychainandsubsequentreleaseofa52aminoacidactivationglycopeptide.FactorXathenservesastheenzymecomponentoftheprothrombinasecomplexwhichisresponsIBLefortherapidconversionofprothrombintothrombin.TheglaresiduesenablefactorX/Xatobindphospholipid(i.e.cellsurfaces)inacalciumdependentmanner;arequirementforassemblyoftheprothrombinasecomplex.ThefirstEGFhomologydomaincontainsaCa2+bindingsitewhichactsasahingetofoldtheEGFandGLAdomainstowardseachother(12).Thisregionofthemoleculeisinvolvedintherecognitionofcellularbindingdomains.

HumanfactorXisisolatedfromfreshfrozenhumanplasmabyacombinationofconventionaltechniques(3)andimmunoaffinitychromatography(4).InadditiontothestandardhumanfactorXpreparation,Gla-domainlesshumanfactorXisalsoavailable.BovinefactorXisisolatedfromfreshbovineplasmausingamodificationoftheprocedurereportedbyBajajetal.(5,6).Thepurifiedzymogenissuppliedin50%(vol/vol)glycerol/H2Oandshouldbestoredat-20oC.PurityisdeterminedbySDS-PAGEanalysisandactivityismeasuredinafactorXclottingassay.

Properties:

Localization	Plasma
Plasmaconcentration	10µg/ml
Modeofaction	Zymogen;precursortotheserineproteasefactorXa
Molecularweight	58,900(human)(7) 55,100(bovine)(8)
Extinctioncoefficient	E 1% 1cm,280nm =11.6(human)(9)     =12.4(bovine)(10)
Isoelectricpoint	4.9-5.2(human)(9) 4.8-5.2(bovine)(9)
Structure	twosubunits,Mr=16,200and42,000(human),Mr=16,500and39,300(bovine),NH2-terminalgladomain,andtwoEGFdomains
Percentcarbohydrate	15%(human)(7) 10%(bovine)(8)
Post-translationalmodifications	elevenglaresidues(7,8) oneβ-hydroxyaspartate

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