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A7512

Sigma-Aldrich

N-Acetyl-DL-phenylalanine β-naphthyl ester

≥98% (TLC), suitable for ligand binding assays

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About This Item

Formule empirique (notation de Hill):
C21H19NO3
Numéro CAS:
20874-31-1
Poids moléculaire :
333.38
Numéro MDL:
MFCD00037746
Code UNSPSC :
12352209
ID de substance PubChem :
24891248
Nomenclature NACRES :
NA.26

product name

N-Acetyl-DL-phenylalanine β-naphthyl ester,

Pureté

≥98% (TLC)

Forme

powder

Technique(s)

ligand binding assay: suitable

Couleur

white

Température de stockage

2-8°C

Chaîne SMILES 

CC(=O)NC(Cc1ccccc1)C(=O)Oc2ccc3ccccc3c2

InChI

1S/C21H19NO3/c1-15(23)22-20(13-16-7-3-2-4-8-16)21(24)25-19-12-11-17-9-5-6-10-18(17)14-19/h2-12,14,20H,13H2,1H3,(H,22,23)

Clé InChI

BBXRRTJNJCPGBU-UHFFFAOYSA-N

Catégories apparentées

Actions biochimiques/physiologiques

N-Acetyl-DL-phenylalanine β-naphthyl ester (NAPBNE), a chromogenic substrate, is used to identify, differentiate and characterize serine protease(s) and peptidase(s).

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)

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H Y Darani et al.
Parasitology, 115 ( Pt 3), 237-247 (1997-09-23)
A cationic Schistosoma mansoni cercarial antigen was shown to be a serine protease as it was capable of hydrolysing N-acetyl-DL-phenylalanine beta-naphthyl ester (NAPBNE) after precipitation by immunoelectrophoresis, and this reaction was modulated by the serine protease inhibitors phenylmethanesulfonyl fluoride (PMSF)
M A Jongsma et al.
Analytical biochemistry, 212(1), 79-84 (1993-07-01)
An improved, time efficient, visual assay for quantitative determination of proteinase inhibitor activity in protein extracts is reported. Proteinase inhibitor activity of mammalian, bacterial, and fungal serine proteinases can be quantified. The method relies on radial diffusion of proteinase inhibitor
P Collin-Osdoby et al.
Molecular & general genetics : MGG, 243(6), 674-680 (1994-06-15)
Mutations at the apeA locus in Salmonella typhimurium lead to loss of a soluble enzyme ("protease I") that hydrolyzes the chromogenic endoprotease substrate N-acetyl phenylalanine beta-naphthyl ester. We have isolated pseudorevertants of S. typhimurium apeA mutations that have regained the
H Y Darani et al.
Parasitology, 135(4), 467-472 (2008-01-23)
An enzyme found previously in extracts of adult Schistosoma mansoni worms, that hydrolysed the chromogenic substrate N-acetyl-DL-phenylalanine beta-naphthyl-ester, has here been further investigated and characterized. Evidence that the molecule found in the parasite was antigenically and enzymatically homologous with a
K Havemann et al.
Klinische Wochenschrift, 61(1), 49-56 (1983-01-03)
Two cytochemical methods for detection of granulocytic elastase and chymotrypsin employing alanine and phenylalanine naphthyl esters were developed. Specificity of reaction with the ester substrates was proven by chloromethyl ketone inhibitors. The results of both staining methods were almost identical
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