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C3637

Sigma-Aldrich

Z-L-Lys-ONp hydrochloride

≥98% (HPLC)

Synonyme(s) :

N2-[(phenylmethoxy)carbonyl]-L-lysine 4-nitrophenyl ester hydrochloride (1:1) 

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About This Item

Formule empirique (notation de Hill):
C20H23N3O6 · HCl
Numéro CAS:
2179-15-9
Poids moléculaire :
437.87
Numéro CE :
218-546-5
Numéro MDL:
MFCD00039055
Code UNSPSC :
12352209
eCl@ss :
32160406
ID de substance PubChem :
24892631
Nomenclature NACRES :
NA.26

product name

Z-L-Lys-ONp hydrochloride,

Pureté

≥98% (HPLC)

Niveau de qualité

200

Forme

powder

Couleur

white to off-white

Solubilité

methanol: 50 mg/mL, clear, colorless to faintly yellow

Température de stockage

−20°C

Chaîne SMILES 

Cl[H].NCCCC[C@H](NC(=O)OCc1ccccc1)C(=O)Oc2ccc(cc2)[N+]([O-])=O

InChI

1S/C20H23N3O6.ClH/c21-13-5-4-8-18(22-20(25)28-14-15-6-2-1-3-7-15)19(24)29-17-11-9-16(10-12-17)23(26)27;/h1-3,6-7,9-12,18H,4-5,8,13-14,21H2,(H,22,25);1H/t18-;/m0./s1

Clé InChI

JFZLPXVXTZKFDV-FERBBOLQSA-N

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Application

Z-L-Lys-ONp hydrochloride has been used as a substrate for trypsin to monitor hydrolysis reaction using mass spectroscopy studies.

Actions biochimiques/physiologiques

N-α-carbobenzoxy-L-lysine-p-nitrophenyl ester (Z-L-Lys-ONp) is a para-nitrophenol ester of N-CBZ-L-lysine. Z-L-Lys-ONp and other N-CBZ-amino acid p-nitrophenol esters are chromogenic substrates used for the differentiation and characterization of proteases and endopeptidases. It acts as a substrate for bromelain.

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

M F Pardo et al.
Journal of agricultural and food chemistry, 48(9), 3795-3800 (2000-09-20)
A new plant endopeptidase was obtained from unripe fruits of Bromelia balansae Mez (Bromeliaceae). Crude extracts were partially purified by ethanol fractionation. This preparation (redissolved ethanol precipitate, REP) showed maximum activity at pH 8.8-9.2, was very stable even at high
Paul V Attwood et al.
Analytical biochemistry, 334(2), 382-389 (2004-10-21)
Mass spectrometry offers a potential means of measuring virtually all enzyme-catalyzed reactions by simultaneously measuring the concentrations of substrates, products, and intermediates where there are differences in mass between them. To perform these measurements the reaction mixture must be aged
M F Pardo et al.
Biological chemistry, 382(5), 871-874 (2001-08-24)
Unripe fruit extracts of Bromelia balansae Mez (Bromeliaceae), whose principal endopeptidase is balansain I (isolated for anion exchange chromatography: pI = 5.45, molecular weight = 23192), exhibit a pH profile with a maximum activity around pH 9.0 and are inhibited
Susana R Morcelle et al.
Fitoterapia, 75(5), 480-493 (2004-07-21)
As part of a screening of latex endopeptidases from plants growing in Argentina, the presence of proteolytic activity in the latex of Funastrum clausum stems is reported. The proteases present in the crude extract showed the main characteristics of the
N E Mackenzie et al.
The Biochemical journal, 219(2), 437-444 (1984-04-15)
The kinetics of the trypsin-catalysed hydrolysis of the highly specific substrate N alpha-benzyloxycarbonyl-L-lysine p-nitrophenyl ester were studied under cryoenzymological conditions by 13C-n.m.r. spectroscopy at pH approx. 3.0. The kinetics of this reaction are shown to be in agreement with similar
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