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Merck
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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

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

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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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
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
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
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
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