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Key Documents

SCP0225

Sigma-Aldrich

Proteasome Substrate

≥95% (HPLC), lyophilized

Synonyme(s) :

Carbobenzoxy-Gly-Gly-Leu-7-amido-4-methylcoumarin, benzyloxycarbonyl-glycyl-glycyl-leucyl-7-amido-4-methylcoumarin, Z-GGL-AMC

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About This Item

Formule empirique (notation de Hill):
C28H32N4O7
Poids moléculaire :
536.58
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.32

product name

Proteasome Substrate,

Pureté

≥95% (HPLC)

Forme

lyophilized

Composition

Peptide Content, ≥87%

Conditions de stockage

protect from light

Température de stockage

−20°C

Amino Acid Sequence

Z-Gly-Gly-Leu-AMC

Application

Z-Gly-Gly-Leu-7-amido-4-methylcoumarin (Z-Gly-Gly-Leu-AMC) has been used as a substrate for proteasome peptidase to measure proteosome activities using spectrophotometer.

Actions biochimiques/physiologiques

Z-Gly-Gly-Leu-7-amido-4-methylcoumarin (Z-Gly-Gly-Leu-AMC) is a fluorogenic peptide that is used in analysis of protease and peptidase activity of proteasomes. Z-GGL-AMC has been noted as a particular substrate for chymotrypsin-like activity. It has low solubility and precipitates at 100μM.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

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Universal Protease Substrate lyophilized, suitable for detection, pkg of 40 mg (40 μmol; 100mM)

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11734334001

Universal Protease Substrate

7-Amino-4-methylcoumarin 99%

Sigma-Aldrich

257370

7-Amino-4-methylcoumarin

István Nagy et al.
Journal of bacteriology, 185(2), 496-503 (2003-01-04)
In a proteasome-lacking mutant of Streptomyces coelicolor A3(2), an intracellular enzyme with chymotrypsin-like activity, absent from the wild type, was detected. Complementation that restored proteasome function did not suppress expression of the endopeptidase. Since the enzyme was not found in
C P Ma et al.
The Journal of biological chemistry, 267(15), 10515-10523 (1992-05-25)
A protein that greatly stimulates the multiple peptidase activities of the 20 S proteasome (also known as macropain, the multicatalytic protease complex, and 20 S protease) has been purified from bovine red blood cells and from bovine heart. The activator
M Rohrwild et al.
Proceedings of the National Academy of Sciences of the United States of America, 93(12), 5808-5813 (1996-06-11)
We have isolated a new type of ATP-dependent protease from Escherichia coli. It is the product of the heat-shock locus hslVU that encodes two proteins: HslV, a 19-kDa protein similar to proteasome beta subunits, and HslU, a 50-kDa protein related
Raymond J. Deshaies
Ubiquitin and Protein Degradation, Part 1, 1 null
S Rathore et al.
Cell death & disease, 2, e231-e231 (2011-11-25)
The ATP-dependent ClpQY protease system in Plasmodium falciparum is a prokaryotic machinery in the parasite. In the present study, we have identified the complete ClpQY system in P. falciparum and elucidated its functional importance in survival and growth of asexual
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