SARS-CoV-2 (2019-nCoV) 3CLpro / 3C-like protease-His & AVI Recombinant Protein


SARS-CoV-2 (2019-nCoV) 3CLpro / 3C-like protease-His & AVI Recombinant Protein: Product Information

> 95 % as determined by SDS-PAGE.
Please contact us for more information.
Protein Construction
A DNA sequence encoding the SARS-CoV-2 (2019-nCoV) 3CL Protease (YP_009725295.1) (Ser3264-Gln3569) was expressed with a N-terminal polyhistidine tagged AVI tag at the N-terminus.
Expressed Host
E. coli
Predicted N Terminal
Molecule Mass
The recombinant SARS-CoV-2 (2019-nCoV) 3CL Protease consists of 328 amino acids and predicts a molecular mass of 36.57 kDa.
Lyophilized from sterile PBS,pH 7.4
Please contact us for any concerns or special requirements.
Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the hard copy of CoA.
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Stability & Storage
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃
Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

SARS-CoV-2 (2019-nCoV) 3CLpro / 3C-like protease-His & AVI Recombinant Protein: Images

CoV 3CLpro / 3C-like protease Background Information

3C-like protease (3CLpro) is the main protease of Humann Coronavirus. 3C-like protease (3CLpro) is a key enzyme, as it cleaves several sites to produce non-structural proteins that are essential for genome replication and Coronavirus virion production, such as an RNA-dependent RNA polymerase, a helicase, ribonucleases and 3CLpro itself, from two types of polyproteins (pp1a and pp1ab). SARS-CoV 3CLpro exists as a homodimer and each protomer has an active site.
  • Tomonari Muramatsu,et al.Autoprocessing mechanism of severe acute respiratory syndrome coronavirus 3C-like protease (SARS-CoV 3CLpro) from its polyproteins.FEBS Journal.2013
  • Ziebuhr J,Molecular biology of severe acute respiratory syndrome coronavirus. Curr Opin Microbiol.2004
  • Yang H, et al. The crystal structures of severe acute respiratory syndrome virus main protease and its complex with an inhibitor. Proc Natl Acad Sci USA.2003
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