SARS-CoV-2 (COVID-19) 3CL-Mpro Protein, unmodified
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SKU: P2020-027 trenzyme
Cysteine protease 3CL-Mpro of SARS-CoV-2 (COVID-19) that cleaves the transcribed viral polyprotein into several functional proteins at two self-cleavage sites.
- Product Name: SARS-CoV-2 (COVID-19) 3CL-Mpro Protein, unmodified
- Catalog No.: P2020-027
- RefSeq Links: NC_045512.2; MN908947.3; YP_009724390.1; QHD43416.1; GeneID: 43740568; UniProt: P0DTD1
- Synonyms: 3CL Mpro; 3CL Pro; 3CL protease; 3C-like main protease; SARS-CoV-2; coronavirus; 2019-nCoV; COVID-2019; COVID-19
“In our COVID-19 projects, we have had very good experience with the SARS-CoV-2 proteins produced by trenzyme: rapid and reliable production of the functional proteins from different cell lines continued to provide first-class support for our projects.”
Dr. Peter Rauch
CANDOR Bioscience GmbH, Wangen, Germany
- Species: SARS-CoV-2; Wuhan seafood market pneumonia virus
- Tags: Tag-free
Sequence without tags (AA 1-306):
- Expression Host: E. coli
- Formulation: PBS, pH 7,4; contains Glycerol as protectant
- Format: Liquid, stored and shipped at -80°C
- Purity: > 90% as determined by SDS-PAGE
The new coronavirus SARS-CoV-2 expresses two proteases, the papain-like protease (PLpro) and 3C-like protease (3CLpro). Both belong to the group of cysteine proteases, as they have a cysteine residue at their catalytic site. Their main function is the processing of the viral polyprotein, that contains two cleavage sites to build up the viral replicase complex. Additionally, PLpro has the ability of removing ISG15 and ubiquitin from viral proteins expressed in the cell, this enables evasion from the innate immune response by the host. This presents an interesting target for drug development, as it would not only inhibit the viral replication but would also prevent the massive immunological response resulting of the over-activation of the host´s immune system, that can lead to damaging of uninfected cells and therefore worsening of the patient´s condition.
Our protein contains no additional amino acids at the N-terminus like proteins from competitors. Therefore, the protease has the authentic N-terminus which is part of the active site of the protein. N-terminal His-Tag was removed by a proteolytic digest producing an authentic N-terminus to ensure highest proteolytic activity.
Histogram of marked lane in gel picture