C0788

Z-Leu-Leu-Glu β-naphthylamide

Name: Z-Leu-Leu-Glu β-naphthylamide
Brand: SIGMA
Price: 342 USD

≥98%, powder

Synonym(s):

Cbz-LLE β-naphthylamine

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50 MG

$342.00

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About This Item

Empirical Formula (Hill Notation):

C₃₅H₄₄N₄O₇

CAS Number:

75873-85-7

Molecular Weight:

632.75

NACRES:

NA.77

PubChem Substance ID:

24892275

UNSPSC Code:

12352209

MDL number:

MFCD00058505

Assay:

≥98%

Form:

powder

Quality level:

200

Key Documents

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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)

SMILES string

CC(C)CC(NC(=O)OCc1ccccc1)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)Nc2ccc3ccccc3c2

InChI key

MIYHULQEZFNUGE-UHFFFAOYSA-N

assay

≥98%

form

powder

color

white

solubility

THF: 25 mg/mL, clear, colorless

storage temp.

−20°C

Quality Level

200

Related Categories

Bioactive Small Molecule Inhibitors

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Show Differences

1 of 4

This Item	L1635	SML1836	C0483
Sigma-Aldrich C0788 Z-Leu-Leu-Glu β-naphthylamide	Sigma-Aldrich L1635 L-Leucine β-naphthylamide	Sigma-Aldrich SML1836 β-ODAP	Sigma-Aldrich C0483 Z-Leu-Leu-Glu-7-amido-4-methylcoumarin
assay ≥98%	assay ≥98% (TLC)	assay ≥98% (HPLC)	assay ≥95%
form powder	form powder	form powder	form solid
Quality Level 200	Quality Level 200	Quality Level 100	Quality Level 200
storage temp. −20°C	storage temp. −20°C	storage temp. 2-8°C	storage temp. −20°C
solubility THF: 25 mg/mL, clear, colorless	solubility H₂O: insoluble	solubility 0.1 M HCl: 2 mg/mL, clear (warmed)	solubility DMSO: soluble
color white	color -	color white to beige	color -

General description

Substrate for the glutamylpeptidyl-peptide hydrolase activity of the 20S proteasome (multicatalytic proteinase complex).

pictograms

GHS08

signalword

Warning

hcodes

H351

pcodes

P281

Hazard Classifications

Carc. 2

Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type P3 (EN 143) respirator cartridges

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Peptidylglutamyl-peptide hydrolase activity of the multicatalytic proteinase complex: evidence for a new high-affinity site, analysis of cooperative kinetics, and the effect of manganese ions.

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

Catalytic components of the bovine pituitary multicatalytic proteinase complex (proteasome).

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

Characterization of recombinant REGalpha, REGbeta, and REGgamma proteasome activators.

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

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

Activation of GluR6-containing kainate receptors induces ubiquitin-dependent Bcl-2 degradation via denitrosylation in the rat hippocampus after kainate treatment.

Jia Zhang et al.

The Journal of biological chemistry, 286(9), 7669-7680 (2010-12-15)

We previously showed that Bcl-2 (B-cell lymphoma 2) is down-regulated in a kainate (KA)-induced rat epileptic seizure model. The underlying mechanism had remained largely unknown, but we here report for the first time that denitrosylation and ubiquitination are involved. Our

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