SARS-CoV-2 (COVID-19) 3CL-Mpro Protein, unmodified
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.
Order Details
- 100µg – 490€
- more on request – bulk and gram quantities available
Shipped next working day, depending on destination
Overview
| 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 |
| Synonyms | 3CL Mpro; 3CL Pro; 3CL protease; 3C-like main protease; SARS-CoV-2; coronavirus; 2019-nCoV; COVID-2019; COVID-19 |
Sequence Information
| Species | SARS-CoV-2; Wuhan seafood market pneumonia virus |
| Tags | tag-free |
| Sequence without tags (AA 1-306) | SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIR KSNHNFLVQAGNVQLRVIGHSMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNG SPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFCYMHHMELPTGVHAGTDLEGN FYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQC SGVTFQ |
Product Information
| 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 |
Background Information
| 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. |
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SDS-PAGE/Coll. Coomassie |
Histogram of marked lane in gel picture |
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Reinhold Horlacher, PhD
Managing Director & CSO
We would be happy to provide you with your desired protein and to support you on your protein research project. If you have any questions or requests, our scientific experts will be happy to answer them shortly.
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