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Inne dokumenty

C9521

Sigma-Aldrich

Z-Phe-Arg 7-amido-4-methylcoumarin hydrochloride

kallikrein substrate, ≥95% (HPLC), powder

Synonim(y):

Z-Phe-Arg-AMC

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About This Item

Wzór empiryczny (zapis Hilla):
C33H36N6O6 · HCl
Numer CAS:
70382-26-2
Masa cząsteczkowa:
649.14
Numer MDL:
MFCD00077030
Kod UNSPSC:
12352204
Identyfikator substancji w PubChem:
24893165
NACRES:
NA.32

product name

Z-Phe-Arg 7-amido-4-methylcoumarin hydrochloride, kallikrein substrate

Próba

≥95% (HPLC)

Postać

powder

stężenie

≥95%

rozpuszczalność

methanol: 20 mg/mL, clear, colorless

temp. przechowywania

−20°C

ciąg SMILES

O=C(N[C@@H](CC1=CC=CC=C1)C(N[C@@H](CCCNC(N)=N)C(NC2=CC=C(C(C)=CC(O3)=O)C3=C2)=O)=O)OCC4=CC=CC=C4.[Cl]

InChI

1S/C33H36N6O6/c1-21-17-29(40)45-28-19-24(14-15-25(21)28)37-30(41)26(13-8-16-36-32(34)35)38-31(42)27(18-22-9-4-2-5-10-22)39-33(43)44-20-23-11-6-3-7-12-23/h2-7,9-12,14-15,17,19,26-27H,8,13,16,18,20H2,1H3,(H,37,41)(H,38,42)(H,39,43)(H4,34,35,36)

Klucz InChI

ZZGDDBWFXDMARY-UHFFFAOYSA-N

Opis ogólny

Z-Phe-Arg 7-amido-4-methylcoumarin (Z-FR-AMC) is a peptidomimetic substrate for papainand other enzymes such as cathepsin K. It is also a fluorogenic synthetic peptide for the enzymes cathepsins L and B.

Zastosowanie

Z-Phe-Arg 7-amido-4-methylcoumarin hydrochloride has been used:
  • as a fluorogenic substrate in actinidin inhibition assay
  • as a kallikrein substrate
  • as a trypsin substrate for fluorometric assay
  • as a cathepsin-L substrate

Działania biochem./fizjol.

Z-Phe-Arg 7-amido-4-methylcoumarin (Z-FR-AMC) proteolytic lysis by proteases leads to the liberation of AMC resulting in increased fluorescence in the enzymatic reaction.

Substraty

A fluorogenic substrate for plasma kallikrein.
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Kod klasy składowania

11 - Combustible Solids

Klasa zagrożenia wodnego (WGK)

WGK 3

Temperatura zapłonu (°F)

Not applicable

Temperatura zapłonu (°C)

Not applicable

Środki ochrony indywidualnej

Eyeshields, Gloves, type N95 (US)

Certyfikaty analizy (CoA)

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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

L Troeberg et al.
Immunopharmacology, 36(2-3), 295-303 (1997-06-01)
Anti-peptide antibodies were produced against the cysteine proteinase trypanopain-Tb from Trypanosoma brucei brucei and the effects of these antibodies on enzyme activity against carboxybenzoyl (Z)-Phe-Arg-aminomethylcoumarin (AMC) investigated. A peptide was synthesised corresponding to a region of the trypanopain-Tb active site
L Salvati et al.
European journal of biochemistry, 268(11), 3253-3258 (2001-06-08)
Cysteine proteinases are relevant to several aspects of the parasite life cycle and of parasite-host relationships. Here, a quantitative investigation of the effect of temperature and pH on the total substrate inhibition of cruzipain, the major papain-like cysteine proteinase from
Cinthia Bernardes Gomes et al.
Biochimie, 133, 28-36 (2016-12-07)
Leishmania (Viannia) braziliensis presents adaptive protease-dependent mechanisms, as cysteine proteinases B (CPB). This study investigates the expression of three cpb gene isoforms and CPB enzymatic activity during the parasite differentiation. Relative expression levels of LbrM.08.0810 gene were assessed, exhibiting a
E Dufour et al.
Biochemistry, 34(28), 9136-9143 (1995-07-18)
Enzymes efficiently catalyze reactions by stabilizing inherently unstable transition states. For cysteine proteases, part of the stabilization is provided by a region of the enzyme termed the oxyanion hole. Site-directed mutagenesis has been used to investigate further the role of
Early ontogenetic development, digestive enzymatic activity and gene expression in red sea bream (Pagrus major)
Khoa TND, et al.
Aquaculture (Amsterdam, Netherlands), 512, 734283-734283 (2019)
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