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

DomainStructureofHumanFactorVII
ThedomainstructureofhumanfactorVIIisrepresented,where:GLA=regioncontainingγ-carboxyglutamicacidresidues,EGF=regioncontainingsequenceshomologoustohumanepidermalgrowthfactor,CATALYTICDOMAIN=regioncontainingtheserineproteasecatalytictriad.ThesiteatwhichfactorXacleavesfactorVIItoformfactorVIIaisindicatedwithanarrow.

SampleGelInformation:

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

Overview:

HumanfactorVIIisasinglechain,vitaminK-dependent,plasmaglycoproteinwhichissynthesizedintheliver(1-3).Priortosecretionintotheblood,posttranslationalmodificationbyavitaminK-dependentcarboxylaseproducesten-carboxyglutamicacid(gla)residueslocatedintheNH2-terminalportionofthemolecule,whichfacilitatecellmembranebinding.FactorVIIisproteolyticallyactivatedtotheserineprotease,factorVIIa,duringcoagulation.FactorVIIcanbeactivatedbythrombin,factorIXa,factorXaorfactorXIIa.TheactivationresultsincleavageofthesinglechainmoleculeontheCOOH-terminalsideofarginine-152,toproduceanNH2-terminalderivedlightchain(Mr=20,000)andaCOOH-terminalderivedheavychain(Mr=30,000)whichremaincovalentlyassociatedbyasingledisulfidebond.Thelightchainregioncontainsthegladomain,aswellastwogrowthfactordomainswhicharehomologoustohumanepidermalgrowthfactor(EGF).Asingleβ-hydroxyasparticacididentifiedinfactorVIIisalsolocatedinthelightchainregion.TheheavychainregionoffactorVIIacontainsthecatalyticdomain.FactorVIIaandthecofactor,tissuefactor,maycombineonnegativelychargedcellsurfacesinacalciumdependentmannertoformtheextrinsicfactorXaseenzymecomplex.ThisenzymecomplexcatalyzestheconversionofbothfactorIXtofactorIXaandfactorXtofactorXa.TheCDNAforfactorVIIhasbeenisolatedandthenucleotidesequencedetermined(4).FactorVIIsharesextensivesequencehomologywithotherserineproteasesincludingfactorIX,factorXandproteinC.

HumanfactorVIIispurifiedusingacombinationofconventionaltechniques(2)andimmunoaffinitychromatography(5).Thepurifiedproteinissuppliedin50%(vol/vol)glycerol/H2Oandshouldbestoredat-20oC.PurityisdeterminedbySDS-PAGEanalysisandactivityismeasuredinafactorVIIclottingassay.

Properties:

Localization	Plasma
Plasmaconcentration	0.5µg/ml(2)-(baseduponactivitymeasurements)
Modeofaction	Zymogen;precursortotheserineproteasefactorVIIa
Molecularweight	50,000(2)
Extinctioncoefficient	E 1% 1cm,280nm =13.9
Isoelectricpoint	4.8-5.1(6)-(baseduponanalysisofbovinefactorVII)
Structure	singlechain,NH2-terminalgla-domain,twoEGFdomains
Percentcarbohydrate	13%(7)-(baseduponanalysisofbovinefactorVII)
Post-translationalmodifications	oneβ-hydroxyaspartate(8),tenglaresidues(9)

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