SARS-CoV-2 (2019-nCoV) NSP7-Recombinant Protein


SARS-CoV-2 (2019-nCoV) NSP7-Recombinant Protein: Product Information

> 90 % as determined by SDS-PAGE.
Please contact us for more information.
Testing in progress
Protein Construction
A DNA sequence encoding the SARS-CoV-2 (2019-nCoV) NSP7 Protein (YP_009725303.1) (Ser1-Gln83) was expressed with two amino acids (GP) at the N-terminus.
Expressed Host
E. coli
Predicted N Terminal
Molecule Mass
The recombinant SARS-CoV-2 (2019-nCoV) NSP7 protein consists of 85 amino acids and predicts a molecular mass of 9.4 kDa.
Lyophilized from sterile 20 mM Tris, 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) NSP7-Recombinant Protein: Images

Coronavirus NSP7 Background Information

NSP7 is conserved within the coronaviridae. NSP7 is a component of the coronavirus replicase polyprotein to comprise a repilication complex. NSP7 has been shown to interact with NSP10 and NSP1 which indicate that NSP7 has a founction in coronavirus-specific RNA replication mechanisms.
  • Wolfgang Peti, et al.Structural Genomics of the Severe Acute Respiratory Syndrome Coronavirus: Nuclear Magnetic Resonance Structure of the Protein nsP7.JOURNAL OF VIROLOGY.2005
  • Yibei Xiao,et al.Nonstructural proteins 7 and 8 of feline coronavirus form a 2:1 heterotrimer that exhibits primer-independent RNA polymerase activity. J Virol. 2012
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