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Merck
CN

B3279

Nα-Benzoyl-L-arginine 4-nitroanilide hydrochloride

proteolytic enzyme substrate, chromogenic, ≥98% (HPLC), powder

Synonym(s):

L-BAPA, L-BAPNA, BANI

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About This Item

Empirical Formula (Hill Notation):
C19H22N6O4 · HCl
CAS Number:
21653-40-7
Molecular Weight:
434.88
NACRES:
NA.32
PubChem Substance ID:
24891697
UNSPSC Code:
12352204
EC Number:
244-505-6
MDL number:
MFCD00063682
Beilstein/REAXYS Number:
4081878

Key Documents

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Product Name

Nα-Benzoyl-L-arginine 4-nitroanilide hydrochloride, ≥98% (HPLC)

InChI

1S/C19H22N6O4.ClH/c20-19(21)22-12-4-7-16(24-17(26)13-5-2-1-3-6-13)18(27)23-14-8-10-15(11-9-14)25(28)29;/h1-3,5-6,8-11,16H,4,7,12H2,(H,23,27)(H,24,26)(H4,20,21,22);1H/t16-;/m0./s1

InChI key

DEOKFPFLXFNAON-NTISSMGPSA-N

SMILES string

Cl[H].NC(=N)NCCC[C@H](NC(=O)c1ccccc1)C(=O)Nc2ccc(cc2)[N+]([O-])=O

assay

≥98% (HPLC)

form

powder

solubility

acetone: water (1:1): 40.00-51.00 mg/mL, clear, colorless to yellow

storage temp.

−20°C

Quality Level

200

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Application

Nα-Benzoyl-L-arginine 4-nitroanilide hydrochloride has been used as substrate:
  • to measure papain activity in spectrophotometric amidase assay
  • to measure the inhibitory function of human cystatin C (HCC) on the protease activity of papain by colorimetric assay
  • for trypsin

General description

Chromogenic substrate for trypsin and other proteolytic enzymes.
Na-Benzoyl-L-arginine 4-nitroanilide hydrochloride (L-BAPNA) is a colorless, chromogenic substrate for proteolytic enzymes such as trypsin, actinidin, and papain.

Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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Certificates of Analysis (COA)

Lot/Batch Number
0000517039
0000510616
0000517039
0000510616
0000455841

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A chemical approach for detecting sulfenic acid-modified proteins in living cells
Reddie KG, et al.
Molecular Biosystems, 4(6), 521- 531 (2008)
Efficient expression, purification and characterization of native human cystatin C in Escherichia coli periplasm
Zhou Y, et al.
Protein Expression and Purification, 111, 18- 22 (2015)
Isolation, expression and characterization of a novel dual serine protease inhibitor, OH-TCI, from king cobra venom
He YY, et al.
Peptides, 29(10), 1692- 1699 (2008)
Daniele O B Sousa et al.
Nutrients, 7(7), 6038-6054 (2015-07-25)
The biochemical and nutritional attributes of two soybean (Glycine max (L.) Merr.) cultivars, one susceptible (Seridó) and the other resistant (Seridó-RCH) to stem canker, were examined to assess whether the resistance to pathogens was related to levels of antinutritional and/or
Raquel O Rocha et al.
Journal of agricultural and food chemistry, 63(22), 5335-5343 (2015-06-03)
Several studies have described the effects of seed exudates against microorganisms, but only few of them have investigated the proteins that have defensive activity particularly against nematode parasites. This study focused on the proteins released in the exudates of soybean
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