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B4500

Sigma-Aldrich

Nα-Benzoyl-L-arginine ethyl ester hydrochloride

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

Synonyme(s) :

BAEE

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About This Item

Formule empirique (notation de Hill):
C15H22N4O3 · HCl
Numéro CAS:
Poids moléculaire :
342.82
Numéro Beilstein :
3781694
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352204
ID de substance PubChem :
Nomenclature NACRES :
NA.32

product name

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

Niveau de qualité

Pureté

≥97% (HPLC)

Forme

powder

Solubilité

water: 50 mg/mL, clear, colorless

Température de stockage

2-8°C

Chaîne 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

Clé InChI

HIXDELXKSSLIKB-YDALLXLXSA-N

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Description générale

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

Substrats

The prototype substrate for trypsin.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

Chensong Pan et al.
Analytical and bioanalytical chemistry, 387(1), 193-204 (2006-11-07)
Matrix-assisted laser desorption/ionization-time-of-flight mass spectrometry (MALDI-TOF-MS) is widely used in a variety of fields because it has the characteristics of speed, ease of use, high sensitivity, and wide detectable mass range for obtaining molecular weights and for structural characterization of
Ying-Qing Yu et al.
Analytical chemistry, 75(21), 6023-6028 (2003-11-01)
Improved in-solution tryptic digestion of proteins in terms of speed and peptide coverage was achieved with the aid of a novel acid-labile anionic surfactant (ALS). Unlike SDS, ALS solubilizes proteins without inhibiting trypsin or other common endopeptidases activity. Trypsin activity
Kinetic and Structural Differentiation of Trypsin from Different Origins
Aithal M, et al.
BioPharm International, 30(1), 38-+-38-+ (2017)
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
Optima of Trypsin-Catalyzed Hydrolysis and Its Inhibition Determined by SDS-PAGE
Zhou X, et al.
Advances in Enzyme Research, 4(01), 1-1 (2016)

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Protocoles

This technical article described the Enzymatic Assay of Trypsin Inhibitor.

Continuous spectrophotometric rate determination method using BAEE substrate measures trypsin activity, essential for enzyme characterization.

Continuous spectrophotometric rate determination method using BAEE substrate measures trypsin activity, essential for enzyme characterization.

Continuous spectrophotometric rate determination method using BAEE substrate measures trypsin activity, essential for enzyme characterization.

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