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SAE0172
Mpro, 3CL Protease from coronavirus SARS-COV-2
recombinant protein, lyophilized product
Synonim(y):
2019-nCoV, 3C Like proteinase, 3C-like main protease, 3CL Mpro, 3CL protease, 3CL proteinase, 3CLpro, COVID-19, COVID-2019, SARS-CoV-2, coronavirus
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About This Item
Kod UNSPSC:
12352204
NACRES:
NA.54
Polecane produkty
Poziom jakości
Formularz
lyophilized
numer dostępu NCBI
Warunki transportu
wet ice
temp. przechowywania
−20°C
Opis ogólny
Mpro, 3CL is a critical enzyme for the virus life cycle. It activity yield non-structural proteins that are crucial for genome replication and Coronavirus virion production: RNA-dependent RNA polymerase, a helicase, ribonucleases and 3CLpro itself, from two types of polyproteins (pp1a and pp1ab).The maturation of SARS-Cov2 virus (SARS coronavirus) depends on cleavage of the overlapping large polyproteins 1a and 1ab by two viral proteases:
SARS-CoV Mpro, 3CL exists as a homodimer and each protomer has an active site. The proteolytic cleavage of 1ab polyprotein by Mpro occurs at 11 sites: 7 sites within the 1a polyprotein, and 11 sites within the 1ab polyprotein. This results in maturation of 16 viral non-structural proteins.Mpro protease forms a functional homodimer. Both the N-terminus and the C- terminus of Mpro have been shown to be critical for dimer formation and for enzyme function.
The Mpro protease, 3CLpro is an ideal target for antiviral drug design due to its high conservation between different coronavirus strains and absence of functional analogs in the human proteome. Mpro protease from SARS-CoV1 and SARS-CoV2 are functionally identical.
- Mpro (main protease)
- PLpro (Papain-like protease)
SARS-CoV Mpro, 3CL exists as a homodimer and each protomer has an active site. The proteolytic cleavage of 1ab polyprotein by Mpro occurs at 11 sites: 7 sites within the 1a polyprotein, and 11 sites within the 1ab polyprotein. This results in maturation of 16 viral non-structural proteins.Mpro protease forms a functional homodimer. Both the N-terminus and the C- terminus of Mpro have been shown to be critical for dimer formation and for enzyme function.
The Mpro protease, 3CLpro is an ideal target for antiviral drug design due to its high conservation between different coronavirus strains and absence of functional analogs in the human proteome. Mpro protease from SARS-CoV1 and SARS-CoV2 are functionally identical.
Cechy i korzyści
Mpro, 3CL Protease (3C-like protease)is the main protease of Human Coronavirus SARS-CoV-2. Mpro 3CL Protease is a cysteine protease. Mpro protease cleaves proteins with sequences including LQ[S/A/G) c-terminal to the glutamine residue.
Postać fizyczna
The product is supplied lyophilized from 20 mM HEPES, 2.5% Trehalose, and 0.05% Tween 20
This product contains the complete sequence of Mpro protease (Accession: YP_009725301.1) without any additional tags. The product is supplied lyophilized from 20 mM HEPES, 2.5% Trehalose, and 0.05% Tween 20.
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Hasło ostrzegawcze
Danger
Zwroty wskazujące rodzaj zagrożenia
Zwroty wskazujące środki ostrożności
Klasyfikacja zagrożeń
Resp. Sens. 1
Kod klasy składowania
11 - Combustible Solids
Klasa zagrożenia wodnego (WGK)
WGK 3
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Certyfikaty analizy (CoA)
Lot/Batch Number
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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.
Huifang Li et al.
Journal of agricultural and food chemistry, 69(41), 12197-12208 (2021-09-30)
Severe acute respiratory syndrome coronavirus (SARS-CoV-2) main protease (Mpro) inhibitors are considered as potential treatments for coronavirus disease 2019, and dietary polyphenols show promise in SARS-CoV-2 Mpro inhibition based on in silico studies. In the present study, we utilize a
Bhupesh Goyal et al.
ACS combinatorial science, 22(6), 297-305 (2020-05-14)
A new coronavirus (CoV) caused a pandemic named COVID-19, which has become a global health care emergency in the present time. The virus is referred to as SARS-CoV-2 (severe acute respiratory syndrome-coronavirus-2) and has a genome similar (∼82%) to that
Chavan Sakshi et al.
Journal of biomolecular structure & dynamics, 1-14 (2021-01-12)
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