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Key Documents

C3022

Sigma-Aldrich

Z-Gly-Gly-Leu p-nitroanilide

protease substrate

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About This Item

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

Assay

≥98% (TLC)

form

powder

solubility

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

storage temp.

−20°C

SMILES string

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

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)

InChI key

IHRYETONKBXGOF-UHFFFAOYSA-N

Substrates

A sensitive chromogenic substrate for subtilisins and neutral endopeptidases.

Storage Class Code

13 - Non Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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A new chromogenic substrate for subtilisin.
L A Lyublinskaya et al.
Analytical biochemistry, 62(2), 371-376 (1974-12-01)
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)
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
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
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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