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.

SDS-PAGE/Coll. Coomassie

Histogram of marked lane in gel picture

SDS-PAGE of 3CL-Mpro unmodified Histogram (of marked lane in gel picture) of 3CL-Mpro Protein-unmodified

 

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Reinhold Horlacher, PhD

Reinhold Horlacher, PhD

Managing Director & CSO

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