- SpeciesReactivityHuman
- SpecificityDetectshumanPRELPindirectELISAsandWesternblots.
- SourcePolyclonalSheepIgG
- PurificationAntigenAffinity-purified
- ImmunogenChinesehamsterovarycelllineCHO-derivedrecombinanthumanPRELP
Gln21-Ile382
Accession#P51888 - FormulationLyophilizedfroma0.2μmfilteredsolutioninPBSwithTrehalose.*Smallpacksize(SP)issuppliedasa0.2µmfilteredsolutioninPBS.
- EndotoxinLevel<0.10 eu="" per="" 1="" μg="" of="" the="" antibody="" by="" the="" lal="">
- LabelUnconjugated
- WesternBlot1µg/mLSeebelow
- Immunocytochemistry5-15µg/mLSeebelow
- NeutralizationMeasuredbyitsABIlitytoneutralizePRELPinhibitionofTRANCE/TNFSF11/RANK L-inducedosteoclast-likecellformationintheRAW 264.7mousemonocyte/macrophagecellline.Rucci,N.etal.(2009)J.CellBiol.187:669.TheNeutralizationDose(ND50)istypically0.2-1.2 µg/mLinthepresenceof5 µg/mLRecombinantHumanPRELP,5 ng/mLRecombinantMouseTRANCE/TNFSF11/RANK L,and20 ng/mLRecombinantMouseM‑CSF.
- ReconstitutionSterilePBStoafinalconcentrationof0.2mg/mL.
- ShippingTheproductisshippedatambienttemperature.Uponreceipt,storeitimmediatelyatthetemperaturerecommendedbelow.*Smallpacksize(SP)isshippedwithpolarpacks.Uponreceipt,storeitimmediatelyat-20to-70°C
- Stability&StorageUseamanualdefrostfreezerandavoidrepeatedfreeze-thawcycles.
- 12monthsfromdateofreceipt,-20to-70°Cassupplied.
- 1month,2to8°Cundersterileconditionsafterreconstitution.
- 6months,-20to-70°Cundersterileconditionsafterreconstitution.
- Bengtsson,E.etal.(1995)J.Biol.Chem.270:25639.
- Merline,R.etal.(2009)J.CellCommun.Signal.3:323.
- McEwan,P.A.etal.(2006)J.Struct.Biol.155:294.
- Neame,P.J.etal.(1999)Cell.Mol.LifeSci.55:1327.
- Grover,J.etal.(1996)Genomics38:109.
- SwissProt#P51888.
- Bengtsson,E.etal.(2000)J.Biol.Chem.275:40695.
- Rucci,N.et.al.(2009)J.CellBiol.187:669.
- Malmsten,M.etal.(2006)MatrixBiol.25:294.
- Grover,J.&P.J.Roughley(2001)MatrixBiol.20:555.
- Bengtsson,E.etal.(2002)J.Biol.Chem.277:15061.
- LongName:Proline-arginine-RichEndLeucine-richrepeatProtein
- EntrezGeneIDs:5549(Human)
- AlternateNames:55kDaleucine-richrepeatproteinofarticularcartilage;MST161;MSTP161;PRELP;prolarginproteoglycan;Prolargin;prolinearginine-richendleucine-richrepeatprotein;proline/arginine-richendleucine-richrepeatprotein;Proline-arginine-richendleucine-richrepeatprotein;SLRR2A;SLRR2AMGC45323
Background:
PRELP(ProlineaRginine-richEndLeucine-richrepeatProtein;alsoProlargin)isa55‑62 kDasecretedglycoproteinthatbelongstothesmallleucine-richproteoglycan(SLRP)superfamilyofextracellularmatrix(ECM)molecules(1‑4).Withinthisfamily,itisconsideredaclassIImember,implyingthatitisunlikelytoformdimericstructures(3).PRELPissynthesizedasa382aminoacid(aa)precursorthatcontainsa20aasignalsequenceplusa362aamatureregion(1,5).LikeotherSLRPs,PRELPcontainsanN-terminalextension(aa 72‑107)coupledtomultipleLeu-richrepeats(LRRs)(aa 95‑382)(6).UnlikeotherSLRPs,PRELPdoesnotcontainanyproteoglycanchains,anditsN‑terminalextensionishighlybasicincharge.TheN-terminusreportedlybindstonegatively-chargedheparin/heparin-sulfate,chondroitinsulfate,andGram-bacterialcellwalls,whiletheLRRregionparticipatesinprotein-proteininteractions(7‑9).AlthoughPRELPisknowntobesynthesizedbyonlyafewcelltypes,includingosteoblasts,skeletalmuscleandchondrocytes,itsexpressionislikelytobemorewidespread,givenitspresenceinthebasementmembrane(BM)ofBowman’scapsule,epididymalepitheliumandthestratifiedsquamousepitheliumoftheskin(1, 10, 11).ThedualbindingprofileofPRELPiskeytoitsfunction.Incartilage,PRELPlikelylinkschondrocytecellmembraneheparinsulfate(HS)chainstoendogenoustypeIIcollagen.WithinthecontextoftheBM,PRELPlikelyplaysananchoringrole.TheBMiscomposedoftype IVcollagenandlaminin,linkedtogetherbynidogen.BMPerlecanreinforcesthislinkagebybindingtoallthreecomponents.PRELP,ontheedgeoftheBM,canbindtofreeperlecanHSchains(viaitsN-terminus),andtounderlyingtypeIcollagen(viaitsLRRs),thusformingananchorfortheBM(11).Notably,theN-terminusappearstodomorethansimplyprovidepartofalinkagemechanism.Inbone,osteoblastsecretedPRELPishypothesizedtoundergoproteolysisbyenzymessuchasLysCandglutamylendopeptidase.Thiswillgenerate40‑75 aaN‑terminalfragmentsthatcanbindtochondroitinsulfateadductsthatexistonthesurfaceofprefusionosteoclastprecursors.Followingbinding,PRELPisinternalized,complexedtoannexin-II,andtranslocatedtothenucleus,whereitinteractswithNFkappaBp65toblockosteoclastmaturation(8).Intissue,PRELPmayalsoundergoproteolyticprocessingduringinflammationtoreleaseanN‑terminalfragmentcontainingaa 21‑42oftheprecursor(7).Thissequencehasbeenshowntopossesspotentantimicrobialactivitybycreatingporesinbacterialcellwalls.MaturehumanPRELPshares91%aaidentitywithmousePRELP(10).
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