Description:

FormerChromogenixsubstrateS-2586nowhasasanidenticalreplacementproduct,DiapharmaCS–PSA(KLK3),productnumberDPG586-25.

DiaPharmaCS–PSA(KLK3)isachromogenicpeptidesubstrateforchymotrypsinandprostatespecificantigen(PSA).DiaPharmaCS–PSA(KLK3)maybeusedforassaying(1)purifiedpreparationsofchymotrypsin,(2)chymotrypsin-likeactivityinBIOLOGicalsamples,and(3)anti-chymotrypsininbloodplasma.AchymotrypsinactivityresearchmethodusingsubstrateMeO-Suc-Arg-Pro-Tyr-pNAisavailable.

ResearchalsosuggeststhattheMeO-Suc-Arg-Pro-Tyr-pNAchromogenicsubstratecanbeusedinresearching enzymaticprostate-specificantigen(PSA)activity.PSAisachymotrypsin-likeserineproteasebelongingtothehumankallikreinfamily,specificallyknownaskallikrein-relatedpeptidase3(KLK3).AlthoughantigenisusedinthenameandPSAisbestknowninresearching prostatecancer,PSAisanactiveenzymethatisproducedathighlevelsinprostatecancer,buttheroleofitsserineproteaseactivityinprostatecancerremainsamystery.

Composition:

EachvialcontainschromogenicsubstrateMeO-Suc-Arg-Pro-Tyr-pNA•HCl25mgandmannitol40mgaddedasabulkingagent.

CHEMISTRY
MeO-Suc-Arg-Pro-Tyr-pNA•HCl

MW:668.29(withoutHClsalt)

PRINCIPLE
MeO-Suc-Arg-Pro-Tyr-pNA+E→MeO-Suc-Arg-Pro-Tyr-OH+pNA+E

E=Enzyme

Background:

S-2586wasoriginallyusedtostudychymotrypsinactivity:

ThechymotrypsinactivityisdeterminedbyitsamidolyticeffectonthesubstrateMeO-Suc-Arg-Pro-Tyr-pNA(S-2586).Therateatwhichp-nitroaniline(pNA)isreleasedismeasuredphotometricallyat405nm.Thiscanbefollowedonarecorder(initialratemethod)orreadafterstoppingthereactionwithaceticacid(acidstoppedmethod).The correlationbetweenthechangeinabsorbanceperminute(DA/min)orabsorbance(A)andthechymotrypsinactivityislinearinthe0.05-1.0µkat/lor3-60U/lrange.Theamidolyticactivityofdifferentchymotrypsinpreparationsdoesnotnecessarilyparalleltheproteaseactivity.

Prostate-specificantigenisa“chymotrypsin-like”serineprotease:

PSAisbestknownasaprostatecancerbioMarker.Itisaserineproteasethatbelongstothehumankallikreinfamilyandpossessaspecificitysimilartochymotrypsin.Therefore,manystudieshaveshownthatthischromogenicsubstratecanbeusedforstudyingPSAenzymeactivity.PSAmaybeanattractivetargetinprostatecancer,andthereforePSAinhibitorsmayrepresentapromisingclassofresearchcompounds.TheinhibitionofofproteolyticactivityofPSAbyinhibitorscanbemeasuredusing MeO-Suc-Arg-Pro-Tyr-pNAsubstrates.