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Merck
모든 사진(1)

주요 문서

SCP0225

Sigma-Aldrich

Proteasome Substrate

≥95% (HPLC), lyophilized

동의어(들):

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

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크기 선택

5 MG
₩235,277

₩235,277


구입 가능 여부는 고객센터에 문의하십시오.


크기 선택

보기 변경
5 MG
₩235,277

About This Item

실험식(Hill 표기법):
C28H32N4O7
Molecular Weight:
536.58
UNSPSC 코드:
12352204
NACRES:
NA.32

₩235,277


구입 가능 여부는 고객센터에 문의하십시오.

제품명

Proteasome Substrate,

분석

≥95% (HPLC)

양식

lyophilized

구성

Peptide Content, ≥87%

저장 조건

protect from light

저장 온도

−20°C

Amino Acid Sequence

Z-Gly-Gly-Leu-AMC

애플리케이션

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]

생화학적/생리학적 작용

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]

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable


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이미 열람한 고객

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
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

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