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B4875

Sigma-Aldrich

Nα-Benzoyl-DL-arginine 4-nitroanilide hydrochloride

trypsin substrate, chromogenic, elastase substrate, ≥98%, powder

Synonym(s):

Nα-Benzoyl-DL-arginine p-nitroanilide hydrochloride, BANI, BAPNA

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About This Item

Empirical Formula (Hill Notation):
C19H22N6O4 · HCl
CAS Number:
Molecular Weight:
434.88
Beilstein:
4081878
EC Number:
MDL number:
UNSPSC Code:
12352204
PubChem Substance ID:
NACRES:
NA.32

product name

Nα-Benzoyl-DL-arginine 4-nitroanilide hydrochloride, ≥98%

Assay

≥98%

form

powder

color

, white to light yellow to light brown

solubility

DMSO: 50 mg/mL (colorless to dark green-yellow to dark brown-yellow)

storage temp.

−20°C

SMILES string

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

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

InChI key

DEOKFPFLXFNAON-UHFFFAOYSA-N

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General description

Nα-Benzoyl-DL-arginine 4-nitroanilide hydrochloride (DL-BAPNA) is a chromogenic substrate for proteolytic enzymes such as trypsin, amidase, and balterobin. Hydrolysis of DL-BAPNA at the bond between the arginine and the p-nitroaniline moieties releases the chromophore p-nitroaniline, which can be detected by colorimetric analysis.

Application

Nα-Benzoyl-DL-arginine 4-nitroanilide hydrochloride has been used as a substrate for trypsin and elastase in enzyme analysis.

Packaging

Bottomless glass bottle. Contents are inside inserted fused cone.

Substrates

A chromogenic trypsin substrate.

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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Boyd DW
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Anju Singh et al.
Journal of biomolecular structure & dynamics, 1-14 (2017-09-21)
Regulatory regions in human genome, enriched in guanine-rich DNA sequences have the propensity to fold into G-quadruplex structures. On exploring the genome for search of G-tracts, it was interesting to find that promoter of Human Myosin Gene (MYH7) contains a
I Kurtovic et al.
Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology, 143(4), 432-440 (2006-02-07)
A trypsin fraction was isolated from the pyloric ceca of New Zealand farmed chinook salmon (Oncorhynchus tshawytscha) by ammonium sulfate fractionation, acetone precipitation and affinity chromatography. The chinook salmon enzyme hydrolyzed the trypsin-specific synthetic substrate benzoyl-DL-arginine-p-nitroanilide (DL-BAPNA), and was inhibited
Guilherme M Zanatta et al.
Journal of periodontology, 77(3), 498-505 (2006-03-04)
The aim of the present study was to evaluate the clinical effects of one-stage periodontal debridement with an ultrasonic instrument, associated with 0.5% povidone (pvp)-iodine irrigation in patients with chronic periodontitis. Forty-five patients were randomly assigned into three groups: the
Carola Engler et al.
PloS one, 4(5), e5553-e5553 (2009-05-14)
We have developed a protocol to assemble in one step and one tube at least nine separate DNA fragments together into an acceptor vector, with 90% of recombinant clones obtained containing the desired construct. This protocol is based on the

Protocols

Objective: To standardize a procedure for the enzymatic assay of Aprotinin.

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