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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
Recommended Products
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
13 - Non 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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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
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
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