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SCP0225

Sigma-Aldrich

Proteasome Substrate

≥95% (HPLC), lyophilized

Synonym(e):

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

Empirische Formel (Hill-System):
C28H32N4O7
Molekulargewicht:
536.58
UNSPSC-Code:
12352204
NACRES:
NA.32

product name

Proteasome Substrate,

Assay

≥95% (HPLC)

Form

lyophilized

Zusammensetzung

Peptide Content, ≥87%

Lagerbedingungen

protect from light

Lagertemp.

−20°C

Amino Acid Sequence

Z-Gly-Gly-Leu-AMC

Anwendung

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.

Biochem./physiol. Wirkung

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.

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Analysenzertifikate (COA)

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

Roche

11734334001

Protease-Universalsubstrat

7-Amino-4-methylcumarin 99%

Sigma-Aldrich

257370

7-Amino-4-methylcumarin

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
S G Roudiak et al.
Biochemistry, 37(1), 377-386 (1998-02-07)
We have charterized a Mycobacterium smegmatis gene encoding a homolog of the ATP-dependent protease Lon (La). Our identification of a Lon homolog, in conjunction with our previous work, identifies M. smegmatis as the first known example of a eubacterium containing
Jung Wook Lee et al.
The Journal of biological chemistry, 284(48), 33475-33484 (2009-10-06)
HslVU is a bacterial ATP-dependent protease distantly related to eukaryotic proteasomes consisting of hexameric HslU ATPase and dodecameric HslV protease. As a homolog of the 20 S proteasome beta-subunits, HslV also uses the N-terminal threonine as the active site residue.
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