C3022
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
General description
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
Regulatory Information
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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)
Evidence that pituitary cation-sensitive neutral endopeptidase is a multicatalytic protease complex.
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
B J Wagner et al.
Experimental eye research, 38(5), 477-483 (1984-05-01)
Lens neutral proteinase is thought to exhibit primarily endopeptidase activity. We have identified a synthetic endopeptidase substrate which is hydrolyzed by the bovine lens neutral proteinase preparation. Among 11 fluoro- and chromogenic endopeptidase substrates, only carbobenzoxy-glycylglycyl-L-leucyl-p-nitroanilide is effectively hydrolyzed. The
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
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