Formulation	25mMHepes,150mMNaCl,pH7.4
Storage	-80°C
Purity	>95%bySDS-PAGE
ActivityDetermination	N/A
ShelfLife(properlystored)	12months

DomainStructureofBetaThromboglobulin
Thedomainstructureoftheβ-thromboglobulinmonomerisrepresented.Theβ-thromboglobulinmonomerisan8,800molecularweightpeptidewhichisderivedviaNH2-terminalproteolysisofaprecursormoleculeLAPF-4(lowaffinityplateletfactor-4).AlthoughtheCOOH-terminaldomainofβ-thromboglobulinischaracterizedbyaclusteringofbasiclysineresidues,theaffinityofb-thromboglobulinforheparinissignificantlyweakerthanthatofplateletfactor-4.Initsnativestate,β-thromboglobulinisahomotetramerconsistingoffour,identical,noncovalently-

SampleGelInformation:

Gel	Novex4-12%Bis-Tris
Load	Load:HumanBetaThromboglobulin,1µgperlane
Buffer	MES
Standard	SeeBluePlus2;Myosin(188kDa),PhosphorylaseB(98kDa),BSA(62kDa),GlutamicDehydrogenase(49kDa),AlcoholDehydrogenase(38kDa),CarbonicAnhydrase(28kDa),MyoglobinRed(17kDa),Lysozyme(14kDa),Aprotinin(6kDa),Insulin,Bchain(3kDa).

Overview:

β-thromboglobulin(b-TG),isalowmolecularweight,heparin-binding,platelet-derivedprotein(1).Itissimilartoplateletfactor-4(PF-4)inthatitislocalizedwithintheplateletalpha-granuleatlevelsreportedtorangefrom8.1-24.2µgper109platelets(2,3).Therelativeconcentrationofβ-TGinplateletsexceedsthatofplasmaby260,000-fold(4)makingβ-TGaconvenientMarkerofplateletactivation.Structurally,β-TGisanalogoustoPF-4inthat,initsnativestate,β-TGisatetramer(1)consistingoffouridentical8800molecularweightpeptidechains(5).IncontrasttoPF-4,β-TGexhibitsaloweraffinityforheparinandalsoexistsasalargermolecularweightspeciesknownas"lowaffinityPF-4"(LAPF-4)(2).β-TGisderivedfromtheproteolyticremovaloffourNH2-terminalaminoacidresiduesfromaLAPF-4(6,7).Immunologicalscreeningofpartiallyfractionatedsupernatantfromactivatedplateletsrevealedahighlybasicformofβ-TGdistinctfromLAPF-4(7).Thisbasicβ-TGspecies,termedplateletbasicprotein(PBP),wassubsequentlyisolated(8)andlaterconcludedfromimmunological,peptidesequencing,andproteolyticprocessingstudiestobeahighermolecularweightprecursorformofbothLAPF-4andβ-TG(9,10).

 

Thephysiologicalfunctionofβ-TGisnotknown.Whileearlystudiessuggestedthattheprecursorformsofβ-TGweremitogenicformousefibroblasts(8,11),itwaslaterconcludedthatthisactivitywasduetogrowthfactorcontamination(10).β-TGhasalsobeenreportedtoinhibitprostacyclin-I2productionbyendothelialcells(12),however,therelevanceofthiseffecthasbeencalledintoquestion(13,14).Thechemotacticactivityofplateletalpha-granuleproteinsforhumanfibroblastshasbeenattributedtobothPF-4andβ-TG(15).

Humanβ-TGispreparedfromthesupernatantofactivatedplateletsbyheparin-agaroseaffinitychromatographyandgelfiltration(1,2).Thepurifiedproteinissuppliedin25mMHepes,150mMNaClpH7.4andshouldbestoredat-80°C.PurityisassessedbySDS-PAGEanalysis.

Properties:

Localization	plateletalpha-granule(3)
PlasmaConcentration	100-200µg/ml
Modeofaction	heparin-bindingprotein:Plasmaconcentrationusedasamarkerofplateletactivation
Molecularweight	35,800(1)
Extinctioncoefficient	E 1% 1cm,280nm =2.6(calculatedbaseduponaminoacidsequenceandmolecularweight)
Structure	homotetramer(monomer,Mr~8800)(5)

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