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Key Documents

B4500

Sigma-Aldrich

Nα-Benzoyl-L-arginine ethyl ester hydrochloride

trypsin substrate, chromogenic, ≥97% (HPLC), powder

Synonym(s):

BAEE

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About This Item

Empirical Formula (Hill Notation):
C15H22N4O3 · HCl
CAS Number:
Molecular Weight:
342.82
Beilstein/REAXYS Number:
3781694
EC Number:
MDL number:
UNSPSC Code:
12352204
PubChem Substance ID:
NACRES:
NA.32

product name

Nα-Benzoyl-L-arginine ethyl ester hydrochloride, trypsin substrate

Quality Level

assay

≥97% (HPLC)

form

powder

solubility

water: 50 mg/mL, clear, colorless

storage temp.

2-8°C

SMILES string

Cl[H].CCOC(=O)[C@H](CCCNC(N)=N)NC(=O)c1ccccc1

InChI

1S/C15H22N4O3.ClH/c1-2-22-14(21)12(9-6-10-18-15(16)17)19-13(20)11-7-4-3-5-8-11;/h3-5,7-8,12H,2,6,9-10H2,1H3,(H,19,20)(H4,16,17,18);1H/t12-;/m0./s1

InChI key

HIXDELXKSSLIKB-YDALLXLXSA-N

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General description

Nα-Benzoyl-L-arginine ethyl ester hydrochloride is a substrate for trypsin. It is a nonprotein substrate used in spectroscopic assays.

Application

  • N

  • α-Benzoyl-L-arginine ethyl ester hydrochloride has been used as a substrate:
  • in peptidyl arginine deiminase (PPAD) assay in P. gingivalis vesicles
  • for assaying proteolytic activity of enzymatic extracts of papaya plant parts
  • in trypsin activity assay of the tail tendon fascicles from rat

Substrates

The prototype substrate for trypsin.

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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Maria T Dulay et al.
Analytical chemistry, 77(14), 4604-4610 (2005-07-15)
Trypsin is covalently linked to a photopolymerized sol-gel monolith modified by incorporating poly(ethylene glycol) (PSG-PEG) for on-column digestion of N(alpha)-benzoyl-l-arginine ethyl ester (BAEE) and two peptides, neurotensin and insulin chain B. The coupling of the enzyme to the monolith is
The mechanical, structural, and compositional changes of tendon exposed to elastase
Grant TM, et al.
Annals of Biomedical Engineering, 43(10), 2477-2486 (2015)
Weijun Wang et al.
Scientific reports, 9(1), 13630-13630 (2019-09-22)
Cellulases play important roles in the dietary fibre digestion in pigs, and have multiple industrial applications. The porcine intestinal microbiota display a unique feature in rapid cellulose digestion. Herein, we have expressed a cellulase gene, p4818Cel5_2A, which singly encoded a
Reynaldo Villalonga et al.
Biotechnology and bioengineering, 81(6), 732-737 (2003-01-17)
Bovine pancreatic trypsin was modified by the mono-6-amino-6-deoxy derivatives of alpha-, beta-, and gamma-cyclodextrin through a transglutaminase-catalyzed reaction. The trypsin-cyclodextrin conjugates, containing about 3 mol of oligosaccharide per mole of protein, were tested for their catalytic and stability properties. The
Mohammad K Hossain et al.
Colloids and surfaces. B, Biointerfaces, 181, 85-93 (2019-05-28)
Electric current responsive magnetic composite particles are prepared in three steps. In the first step, spherical and mesoporous submicrometer-sized magnetic iron oxide (Fe3O4) core particles are prepared by solvothermal method. Then magnetic Fe3O4 particles are functionalized with amine groups using

Articles

Papain is a cysteine protease of the peptidase C1 family. Papain consists of a single polypeptide chain with three disulfide bridges and a sulfhydryl group necessary for activity of the enzyme.

Protocols

This technical article described the Enzymatic Assay of Trypsin Inhibitor.

This procedure is for products with a specification for Trypsin activity using Na-Benzoyl-L-arginine ethyl ester (BAEE) as a substrate. The procedure is a continuous spectrophotometric rate determination (A253, Light path = 1 cm).

Related Content

Trypsin is an enzyme in the serine protease class that consists of a polypeptide chain of 223 amino acid residues. Multiple sources, grades and formulations of trypsin specifically designed for research applications are available.

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

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