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SML2975

Sigma-Aldrich

Dabcyl-KTSAVLQSGFRKME-Edans trifluoroacetate

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

Synonym(s):

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

Empirical Formula (Hill Notation):
C95H141N25O24S2 · xC2HF3O2
CAS Number:
Molecular Weight:
2081.42 (free base basis)
UNSPSC Code:
12352200
NACRES:
NA.77

product name

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

Quality Level

Assay

≥95% (HPLC)

form

powder

color

light brown to dark red

storage temp.

−20°C

Biochem/physiol Actions

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.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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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
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

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