SecretedhumanHtrA1serineproteaseissupposedtoformoligomersofidenticalproteinchainsasrevealedbyX-rayanalysisforthebacterialHtrAproteinDegP[1].PolypeptidechainsofhumanHtrA1consistofseveraldomains:AnN-terminalinsulin-likegrowthfactordomainisfollowedbyaKazal-typeserineproteaseinhibitordomain,alinkerregion,atrypsin-likeproteasedomainandaPDZdomain.ThefunctionofHtrA1appearscloselylinkedtosignalingbyproteinsoftheTGFßfamily.Duringmouseembryodevelopment,HtrA1islocalizedinspecificareaswheresignalingbyTGFßfamilyproteinsoccurs.HtrA1bindsTGFß,BMP4,Gdf5andactivin.Itinhibitssignalingbythesefactors.ForinhibitionserineproteaseactivityofHtrA1isessential.HtrA1isupregulatedinosteoarthriticcartilage.IncreasedcartilageHtrA1maypossIBLyaggravateosteoarthritisbyantagonizingTGFßandtherebypromotingterminaldifferentiationofarticularchondrocytes.Inlaterstagesoftumorprogression,HtrA1isdownregulated.Asaprotease,HtrA1hydrolyzestypeIIprocollagenα1C-propeptide,decorinandbiglycan.ProteolyticactivityofHtrA1isregulatedbyligandbindingtothePDZdomain.
MolecularForm:
RecombinanthumanHtrA1isexpressedininsectcellswithaC-terminalHis-tagandpurified
frominsectcellculturesupernatants.ThecalculatedMrofsecretedHtrA1is50kDa.HtrA1is
solublizedin50mMTris-HCl,pH7.5,150mMNaCl,5mMCaCl2,0.05%Brij-35.
Purity:
RecombinantHtrA1appearsasamajorproteinofabout53kDinSDS-PAGE(>80%oftotal
protein).MinorbandsofHtrA1fragmentsmaybevisibleintheenzymepreparation.
EnzymaticActivity:
ProteolyticactivityofrecombinanthumanHtrA1isdocumentedbydigestionofß-casein.0.5
mgß-casein/mlarecompletelydigestedby5μg/mLHtrA1within3hoursat37ºC(seefigure
above).
How_To_Use:
RecombinantHtrA1allowsdetailedstudiesofthestructureandfunctionofthisprotease.The
enzymeisusedtoscreenforinhibitorsandtocharacteriseinhibitoractions.Recombinant
HtrA1canalsoserveasstandardinenzymaticandimmunochemicalassays.
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