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Merck
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SCP0225

Sigma-Aldrich

Proteasome Substrate

≥95% (HPLC), lyophilized

别名:

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

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5 MG
$151.00

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5 MG
$151.00

About This Item

经验公式(希尔记法):
C28H32N4O7
分子量:
536.58
UNSPSC代码:
12352204
NACRES:
NA.32

$151.00


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产品名称

Proteasome Substrate,

方案

≥95% (HPLC)

表单

lyophilized

组成

Peptide Content, ≥87%

储存条件

protect from light

储存温度

−20°C

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此商品
C8749SCP0003SCP0096
form

lyophilized

form

film or powder

form

lyophilized

form

lyophilized

storage condition

protect from light

storage condition

-

storage condition

protect from light

storage condition

protect from light

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

composition

Peptide Content, ≥87%

composition

-

composition

Peptide Content, ≥80%

composition

Peptide Content, ≥80%

Amino Acid Sequence

Z-Gly-Gly-Leu-AMC

应用

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.[1]

生化/生理作用

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.[2][3]

储存分类代码

11 - Combustible Solids

WGK

WGK 3

闪点(°F)

Not applicable

闪点(°C)

Not applicable


历史批次信息供参考:

分析证书(COA)

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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
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
Raymond J. Deshaies
Ubiquitin and Protein Degradation, Part 1, 1 null

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