Recombinant SARS-CoV-2 nsp13 His (N-Term) Protein

SDS-Page: Recombinant SARS-CoV-2 nsp13 His (N-Term) Protein [NBP3-07081] - SDS-PAGE Image

• Applications: PAGE

Recombinant SARS-CoV-2 nsp13 His (N-Term) Protein Summary

• Description: A recombinant protein with a His (N-Term) tag corresponding to the amino acids Ala5325-Gln5925 of SARS-CoV-2 nsp13
  
  Source: E.coli
  
  Accession: QHD43415.1
• Protein/Peptide Type: Recombinant Protein
• Gene: ORF1ab
• Purity: >90%, by SDS-PAGE quantitative densitometry by Coomassie Blue Staining

Applications/Dilutions

• Dilutions:
  • SDS-Page
• Theoretical MW: 69.15 kDa.
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.

Packaging, Storage & Formulations

• Storage: Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.
• Buffer: PBS, pH 7.5, 0.02% NLS
• Preservative: No Preservative
• Purity: >90%, by SDS-PAGE quantitative densitometry by Coomassie Blue Staining

Alternate Names for Recombinant SARS-CoV-2 nsp13 His (N-Term) Protein

• helicase
• Non-structural protein 13

Background

SARS-CoV-2 Nonstructural Protein 13 (NSP13) is one of the sixteen nonstructural proteins of severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2), the causative agent of COVID-19 (1). SARS-CoV-2 NSP13 is 601 amino acids (aa) with a theoretical molecular weight of 66.9 kDa (1-3). The amino acid sequence alignment of SARS-CoV and SARS-CoV-2's NSP13 has 99.8% sequence identity and 100% sequence similarity, with only one amino acid residue difference between the two proteins (1). NSP13 is suggested to have helicase activity and unwinds RNA (1,3). Furthermore, NSP13 is suggested to interact with NSP12 and through protein-protein interactions, NSP12 enhances NSP13's helicase activity (1,3,4). Additionally, a SARS-CoV-2 interactome study reveals NSP13's involvement in several processes including transcriptional regulation, Golgi organization, protein kinase A signaling, and centrosome complex formation (2). Given its role in centrosome organization, NSP13 is a possible molecular link for the loss of smell, called anosmia, due to the olfactory cilia defects that can occur because of COVID-19 infection (5). NSP13 also interacts with innate immune pathways including the interferon pathway and NF-kappaB pathway (2).

References

1. Yoshimoto F. K. (2020). The Proteins of Severe Acute Respiratory Syndrome Coronavirus-2 (SARS CoV-2 or n-COV19), the Cause of COVID-19. The Protein Journal. https://doi.org/10.1007/s10930-020-09901-4

2. Gordon, D. E., Jang, G. M., Bouhaddou, M., Xu, J., Obernier, K., White, K. M., O'Meara, M. J., Rezelj, V. V., Guo, J. Z., Swaney, D. L., Tummino, T. A., Huttenhain, R., Kaake, R. M., Richards, A. L., Tutuncuoglu, B., Foussard, H., Batra, J., Haas, K., Modak, M., Kim, M., ... Krogan, N. J. (2020). A SARS-CoV-2 protein interaction map reveals targets for drug repurposing. Nature. https://doi.org/10.1038/s41586-020-2286-9

3. Qiu, Y., & Xu, K. (2020). Functional studies of the coronavirus nonstructural proteins. STEMedicine. https://doi.org/10.37175/stemedicine.v1i2.39

4. Romano, M., Ruggiero, A., Squeglia, F., Maga, G., & Berisio, R. (2020). A Structural View of SARS-CoV-2 RNA Replication Machinery: RNA Synthesis, Proofreading and Final Capping. Cells. https://doi.org/10.3390/cells9051267

5. Li, W., Li, M., & Ou, G. (2020). COVID-19, cilia, and smell. The FEBS journal. https://doi.org/10.1111/febs.15491

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are guaranteed for 3 months from date of receipt.

Bioinformatics

• Gene Symbol: ORF1ab