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SCP0225

Sigma-Aldrich

Proteasome Substrate

≥95% (HPLC), lyophilized

Synonym(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

Empirical Formula (Hill Notation):
C28H32N4O7
Molecular Weight:
536.58
UNSPSC Code:
12352204
NACRES:
NA.32

product name

Proteasome Substrate,

assay

≥95% (HPLC)

form

lyophilized

composition

Peptide Content, ≥87%

storage condition

protect from light

storage temp.

−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.

Biochem/physiol Actions

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.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificates of Analysis (COA)

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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
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
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
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
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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