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B7632

Sigma-Aldrich

N-Benzoyl-Phe-Val-Arg-p-nitroanilide hydrochloride

chromogenic, protease substrate, ≥98% (TLC), powder

Synonym(s):

N-Benzoyl-L-phenylalanyl-L-valyl-L-arginine-4-nitroanilide hydrochloride

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About This Item

Empirical Formula (Hill Notation):
C33H40N8O6 · HCl
CAS Number:
Molecular Weight:
681.18
Beilstein:
3027332
MDL number:
UNSPSC Code:
12352204
PubChem Substance ID:
NACRES:
NA.32

product name

N-Benzoyl-Phe-Val-Arg-p-nitroanilide hydrochloride, protease substrate

Assay

≥98% (TLC)

form

powder

solubility

methanol: 20 mg/mL, clear, colorless to light yellow

storage temp.

−20°C

SMILES string

Cl.CC(C)[C@H](NC(=O)[C@H](Cc1ccccc1)NC(=O)c2ccccc2)C(=O)N[C@@H](CCCNC(N)=N)C(=O)Nc3ccc(cc3)[N+]([O-])=O

InChI

1S/C33H40N8O6.ClH/c1-21(2)28(40-31(44)27(20-22-10-5-3-6-11-22)39-29(42)23-12-7-4-8-13-23)32(45)38-26(14-9-19-36-33(34)35)30(43)37-24-15-17-25(18-16-24)41(46)47;/h3-8,10-13,15-18,21,26-28H,9,14,19-20H2,1-2H3,(H,37,43)(H,38,45)(H,39,42)(H,40,44)(H4,34,35,36);1H/t26-,27-,28-;/m0./s1

InChI key

PYVSMZDQQUZGPF-JAQKLANPSA-N

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General description

N-Benzoyl-Phe-Val-Arg-p-nitroanilide is a chromogenic protease substrate.

Application

  • N

  • -Benzoyl-Phe-Val-Arg-p-nitroanilide hydrochloride has been used: as a substrate: for trypsin-like enzyme in the soluble and particulate fractions of the hyphae
  • for the thrombin, recombinant and native batroxobin from snake venom
  • for fibrinolytic enzyme aprE2 in amidolytic activity assay

Packaging

Bottomless glass bottle. Contents are inside inserted fused cone.

Substrates

A substrate for trypsin, thrombin and reptilase.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Substrates for determination of trypsin, thrombin and thrombin-like enzymes.
L Svendsen et al.
Folia haematologica (Leipzig, Germany : 1928), 98(4), 446-454 (1972-01-01)
Seon-Ju Jeong et al.
Journal of microbiology and biotechnology, 24(7), 969-978 (2014-04-20)
The aprE2 gene with its prosequence from Bacillus subtilis CH3-5 was overexpressed in Escherichia coli BL21(DE3) by using plasmid pET26b(+). After IPTG induction, active and mature AprE2 was produced when cells were grown at 20°C, whereas inactive and insoluble enzyme
I J Mackie et al.
Thrombosis research, 28(4), 499-507 (1982-11-15)
The Factor VIII content of Factor IX concentrates was investigated by agarose gel electrophoresis which removed the interfering effects of stabilisers and proteolytic enzyme inhibitors. Factor VIII coagulant activity (FVIII C) as measured by clotting and amidolytic methods correlated well
Maxsuell Lucas Mendes Marques et al.
Marine drugs, 17(1) (2018-12-24)
In this study, sulfated polysaccharide-rich extracts were isolated from 22 tropical seaweeds (4 red, 11 brown, and 7 green) found in northeastern Brazil, and evaluated for the role of anticoagulant agents. Fifteen of the extracts showed anticoagulant activity, including all
The hydrolysis of N-benzoyl-L-phenylalanyl-L-valyl-L-arginine-p-nitroanilide and its use as a substrate for the assay of cathepsin B.
J Butterworth et al.
Analytical biochemistry, 106(1), 156-162 (1980-07-15)

Protocols

Thrombin is an endolytic serine protease that selectively cleaves the Arg–Gly bonds of fibrinogen to form fibrin and release fibrinopeptides A and B.

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