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B4500

Sigma-Aldrich

Nα-Benzoyl-L-arginine ethyl ester hydrochloride

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

Sinónimos:

BAEE

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About This Item

Fórmula empírica (notación de Hill):
C15H22N4O3 · HCl
Número de CAS:
2645-08-1
Peso molecular:
342.82
Beilstein:
3781694
Número CE:
220-157-0
Número MDL:
MFCD00012579
Código UNSPSC:
12352204
ID de la sustancia en PubChem:
24891777
NACRES:
NA.32

Nombre del producto

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

Ensayo

≥97% (HPLC)

Formulario

powder

solubilidad

water: 50 mg/mL, clear, colorless

temp. de almacenamiento

2-8°C

cadena SMILES

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

Clave InChI

HIXDELXKSSLIKB-YDALLXLXSA-N

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Descripción general

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

Aplicación

  • 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

Sustratos

The prototype substrate for trypsin.

Código de clase de almacenamiento

11 - Combustible Solids

Clase de riesgo para el agua (WGK)

WGK 3

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable

Equipo de protección personal

Eyeshields, Gloves, type N95 (US)

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Certificados de análisis (COA)

Lot/Batch Number
BCCH1622
0000135115
0000118817
0000118818
0000115477

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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
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Papain, Cysteine Protease, Properties & Products

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.

Protocolos

Enzymatic Assay of Trypsin Inhibitor

Enzymatic Assay of Trypsin Inhibitor

Procedure for Enzymatic Assay of Trypsin (EC 3.4.21.4)

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).

Contenido relacionado

Trypsin Serine Protease Enzyme

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.

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