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Merck
CN

C3022

Z-Gly-Gly-Leu p-nitroanilide

protease substrate

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About This Item

Empirical Formula (Hill Notation):
C24H29N5O7
CAS Number:
53046-98-3
Molecular Weight:
499.52
NACRES:
NA.32
PubChem Substance ID:
24892559
UNSPSC Code:
12352204
MDL number:
MFCD00038383

Key Documents

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InChI

1S/C24H29N5O7/c1-16(2)12-20(23(32)27-18-8-10-19(11-9-18)29(34)35)28-22(31)14-25-21(30)13-26-24(33)36-15-17-6-4-3-5-7-17/h3-11,16,20H,12-15H2,1-2H3,(H,25,30)(H,26,33)(H,27,32)(H,28,31)

SMILES string

CC(C)CC(NC(=O)CNC(=O)CNC(=O)OCc1ccccc1)C(=O)Nc2ccc(cc2)N(=O)=O

InChI key

IHRYETONKBXGOF-UHFFFAOYSA-N

assay

≥98% (TLC)

form

powder

solubility

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

storage temp.

−20°C

General description

A sensitive chromogenic substrate for subtilisins and neutral endopeptidases.

Storage Class

13 - Non Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Regulatory Information

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Certificates of Analysis (COA)

Lot/Batch Number
BCBD0287
BCBS2166V
BCBP4840V
BCBN0137V
BCBJ4836V

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Degradation of bradykinin by isolated neutral endopeptidases of brain and pituitary.
S Wilk et al.
Biochemical and biophysical research communications, 90(1), 1-6 (1979-09-12)
A new chromogenic substrate for subtilisin.
L A Lyublinskaya et al.
Analytical biochemistry, 62(2), 371-376 (1974-12-01)
J R Arbona et al.
Journal of animal science, 71(12), 3301-3306 (1993-12-01)
Within 1 h after slaughter, two 10-g samples of longissimus muscle were obtained from four crossbred beef cattle. Samples were homogenized in three or six volumes of extraction solution that consisted of 50 mM Tris base, 10 mM EDTA, and
Ajay Kumar Shaw et al.
Journal of photochemistry and photobiology. B, Biology, 86(3), 199-206 (2006-11-18)
Enzymatic activity of a proteolytic enzyme Subtilisin Carlsberg (SC) in anionic sodium dodecyl sulfate (SDS) micellar medium has been explored and found to be retarded compared to that in bulk buffer. Circular dichroism (CD) study reveals that SDS, which is
S Wilk et al.
Journal of neurochemistry, 40(3), 842-849 (1983-03-01)
Pituitary cation-sensitive neutral endopeptidase splits peptide bonds on the carboxyl side of hydrophobic amino acids (chymotrypsin-like activity), basic amino acids (trypsin-like activity), and acidic amino acids (peptidyl-glutamyl-peptide bond hydrolyzing activity). All three activities copurify, are inhibited by cations, and reside
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