SML2975
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
CAS号:
分子量:
2081.42 (free base basis)
分類程式碼代碼:
12352200
NACRES:
NA.77
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product name
Dabcyl-KTSAVLQSGFRKME-Edans trifluoroacetate, ≥95% (HPLC)
品質等級
化驗
≥95% (HPLC)
形狀
powder
顏色
light brown to dark red
儲存溫度
−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.
儲存類別代碼
11 - Combustible Solids
水污染物質分類（WGK）
WGK 3
閃點（°F）
Not applicable
閃點（°C）
Not applicable
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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