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96895

Sigma-Aldrich

Z-Lys-ONp hydrochloride

≥98.0% (AT)

Synonym(s):

Nα-Z-L-lysine 4-nitrophenyl ester hydrochloride

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About This Item

Empirical Formula (Hill Notation):
C20H23N3O6 · HCl
CAS Number:
Molecular Weight:
437.87
Beilstein/REAXYS Number:
7191805
EC Number:
MDL number:
UNSPSC Code:
12352200
PubChem Substance ID:
NACRES:
NA.22

assay

≥98.0% (AT)

form

powder

optical activity

[α]20/D −24±1°, c = 1% in DMF

mp

146-152 °C

application(s)

peptide synthesis

storage temp.

−20°C

SMILES string

Cl.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

InChI key

JFZLPXVXTZKFDV-FERBBOLQSA-N

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)


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R J Szawelski et al.
The Biochemical journal, 199(3), 681-692 (1981-12-01)
1. The hydrolyses of the p-nitrophenyl esters of N-benzyloxycarbonylglycine, alpha-N-benzyloxycarbonyl-L-lysine and N-methoxycarbonyl-L-phenylalanylglycine catalysed by papain (EC 3.4.22.2) have been studied in solvents having a variable composition of 2H2O and H2O. 2. kcat., which represents deacylation in the papain-catalysed hydrolysis of
P D Compton et al.
The Journal of biological chemistry, 261(3), 1248-1252 (1986-01-25)
The effect of aqueous methanol cryosolvents on the catalytic and structural properties of bovine trypsin has been investigated. The low freezing points and low viscosities of methanol-based cryosolvents are desirable for a variety of cryoenzymological experiments. Increasing concentrations of methanol
E Antonini et al.
The Journal of biological chemistry, 258(8), 4676-4678 (1983-04-25)
The formation of the bovine beta-trypsin-bovine basic pancreatic trypsin inhibitor (Kunitz) (BPTI) complex was monitored, making use of three different signals: proflavine displacement, optical density changes in the ultraviolet region, and the loss of the catalytic activity. The rates of
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
Z X Wang et al.
Biochimica et biophysica acta, 1388(1), 84-92 (1998-10-17)
The kinetic theory of the substrate reaction during modification of enzyme activity has been applied to study the inactivation kinetics of enzymes by denaturant. However, an important problem related to the determination of the inactivation rate constants has not been

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