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安全信息

SML2975

Sigma-Aldrich

Dabcyl-KTSAVLQSGFRKME-Edans trifluoroacetate

≥95% (HPLC), powder, FRET substrate of SARS-CoV Mpro

别名:

DABCYL-Lys-Thr-Ser-Ala-Val-Leu-Gln-Ser-Gly-Phe-Arg-Lys-Met-Glu-EDANS trifluoroacetate, N2-[4-[[4-(Dimethylamino)phenyl]azo]benzoyl]-L-lysyl-L-threonyl-L-seryl-L-alanyl-L-valyl-L-leucyl-L-glutaminyl-L-serylglycyl-L-phenylalanyl-L-arginyl-L-lysyl-L-methionyl-N-[2-[(5-sulfo-1-naphthalenyl)amino]ethyl]-L-α-glutamine trifluoroacetate

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About This Item

经验公式(希尔记法):
C95H141N25O24S2 · xC2HF3O2
分子量:
2081.42 (free base basis)
UNSPSC代码:
12352200
NACRES:
NA.77

产品名称

Dabcyl-KTSAVLQSGFRKME-Edans trifluoroacetate, ≥95% (HPLC)

质量水平

方案

≥95% (HPLC)

表单

powder

颜色

light brown to dark red

储存温度

−20°C

生化/生理作用

Dabcyl-KTSAVLQSGFRKME-Edans is a fluorescence resonance energy transfer (FRET) substrate for SARS-CoV main protease Mpro (also called 3CLpro) (538 nm with excitation at 355 nm). Dabcyl-KTSAVLQSGFRKME-Edans is suitable to measure protease activity of COVID-19 virus Mpro, SARS-CoV Mpro, and other viruses.

储存分类代码

11 - Combustible Solids

WGK

WGK 3

闪点(°F)

Not applicable

闪点(°C)

Not applicable

法规信息

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分析证书(COA)

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Linlin Zhang et al.
Journal of medicinal chemistry, 63(9), 4562-4578 (2020-02-12)
The main protease of coronaviruses and the 3C protease of enteroviruses share a similar active-site architecture and a unique requirement for glutamine in the P1 position of the substrate. Because of their unique specificity and essential role in viral polyprotein
Thi Thanh Hanh Nguyen et al.
Biotechnology letters, 34(5), 831-838 (2012-02-22)
The 3C-like protease (3CL(pro)) of severe acute respiratory syndrome associated coronavirus (SARS-CoV) is vital for SARS-CoV replication and is a promising drug target. Recombinant 3CL(pro) was expressed in Pichia pastoris GS115 as a 42 kDa protein that displayed a K
Chih-Jung Kuo et al.
Biochemical and biophysical research communications, 318(4), 862-867 (2004-05-19)
SARS main protease is essential for life cycle of SARS coronavirus and may be a key target for developing anti-SARS drugs. Recently, the enzyme expressed in Escherichia coli was characterized using a HPLC assay to monitor the formation of products

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