C0788
Z-Leu-Leu-Glu β-naphthylamide
≥98%, powder
Synonym(s):
Cbz-LLE β-naphthylamine
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10 MG
$79.00
50 MG
$319.00
About This Item
Empirical Formula (Hill Notation):
C35H44N4O7
CAS Number:
Molecular Weight:
632.75
MDL number:
UNSPSC Code:
12352209
PubChem Substance ID:
NACRES:
NA.77
Recommended Products
assay
≥98%
form
powder
color
white
solubility
THF: 25 mg/mL, clear, colorless
storage temp.
−20°C
SMILES string
CC(C)CC(NC(=O)OCc1ccccc1)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)Nc2ccc3ccccc3c2
InChI
1S/C35H44N4O7/c1-22(2)18-29(38-34(44)30(19-23(3)4)39-35(45)46-21-24-10-6-5-7-11-24)33(43)37-28(16-17-31(40)41)32(42)36-27-15-14-25-12-8-9-13-26(25)20-27/h5-15,20,22-23,28-30H,16-19,21H2,1-4H3,(H,36,42)(H,37,43)(H,38,44)(H,39,45)(H,40,41)
InChI key
MIYHULQEZFNUGE-UHFFFAOYSA-N
Amino Acid Sequence
Z-Leu-Leu-Glu-βNA
Substrates
Substrate for the glutamylpeptidyl-peptide hydrolase activity of the 20S proteasome (multicatalytic proteinase complex).
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H Djaballah et al.
Biochemistry, 31(16), 4133-4141 (1992-04-28)
The multicatalytic proteinase (MCP) complex or proteasome is a major nonlysosomal proteinase of eukaryotic cells. The proteinase can cleave peptide bonds on the carboxyl side of hydrophobic, basic, or acidic amino acid residues. These activities have been referred to as
C Realini et al.
The Journal of biological chemistry, 272(41), 25483-25492 (1997-11-05)
Full-length cDNAs for three human proteasome activator subunits, called REGalpha, REGbeta, and REGgamma, have been expressed in Escherichia coli, and the purified recombinant proteins have been characterized. Recombinant alpha or gamma subunits form heptameric species; recombinant beta subunits are found
C Cardozo
Enzyme & protein, 47(4-6), 296-305 (1993-01-01)
The multicatalytic proteinase complex (MPC), also called the proteasome, is a ubiquitous particle (19S) that is required for life. It is found in the cytoplasm and nucleus of all eukaryotic cells where it degrades selected cytosolic and nuclear proteins. It
Lens neutral proteinase preparations hydrolyze glutamoyl bonds.
B J Wagner et al.
Experimental eye research, 40(6), 879-882 (1985-06-01)
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
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