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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/REAXYS Number:
3027332
MDL number:
UNSPSC Code:
12352204
PubChem Substance ID:
NACRES:
NA.32

product name

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

Quality Level

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

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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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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
P C Ring et al.
Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology, 30(8), 1085-1096 (2000-08-10)
Fel d 1, an important allergen from domestic cats, is a significant cause of asthma. In addition to directly promoting IgE synthesis, other biological activities of allergens may contribute to either allergic sensitization or the magnitude of allergic effector responses.
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)
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)

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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