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Merck
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Documentos clave

SCP0225

Sigma-Aldrich

Proteasome Substrate

≥95% (HPLC), lyophilized

Sinónimos:

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

Fórmula empírica (notación de Hill):
C28H32N4O7
Peso molecular:
536.58
UNSPSC Code:
12352204
NACRES:
NA.32

Nombre del producto

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

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Certificados de análisis (COA)

Lot/Batch Number
LH0631

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Universal Protease Substrate

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Sigma-Aldrich

257370

7-Amino-4-methylcoumarin

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
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
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
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