Host: E. coli • AA: 1-113 • Tag: N-terminal His and C-terminal AVI • MW: 15.5 kDa
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SARS-CoV-2 nsp9 (recombinant)

Item No. 31978

Product Insert (PDF)
Technical Information
Synonyms
  • 2019-nCoV nsp9
  • COVID-19 nsp9
  • Severe Acute Respiratory Syndrome Coronavirus 2 nsp9
Purity
≥90% as determined by SDS-PAGE
Source
Recombinant SARS-CoV-2 N-terminal His-tagged and C-terminal AVI-tagged nsp9 expressed in E. coli
Amino Acids
1-113
MW
15.5 kDa
Lyophilized from sterile 50 mM Tris, pH 7.4, with 150 mM NaCl, and 2 mM βME
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    Product Description

    Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is an enveloped positive-stranded RNA virus and the causative agent of COVID-19, a primarily respiratory illness characterized by fever, cough, and shortness of breath that can lead to life-threatening complications.1,2,3,4,5 The SARS-CoV-2 genome contains approximately 30 kilobases and 14 open reading frames (ORFs) that encode four structural proteins: spike, envelope, membrane, and nucleocapsid, as well as 16 non-structural proteins and 9 accessory factors.6 SARS-CoV-2 non-structural protein 9 (nsp9) is an RNA binding protein. In the related virus SARS-CoV, nsp9 is highly conserved and important for RNA binding and viral replication.7 SARS-CoV-2 nsp9, like the nsp9 of SARS-CoV, forms dimers and contains a unique fold region not found in other CoVs. Cayman’s SARS-CoV-2 nsp9 (recombinant) protein consists of 140 amino acids and has a calculated molecular weight of 15.5 kDa.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Kandeel, M., Ibrahim, A., Fayez, M., et alFrom SARS and MERS CoVs to SARS-CoV-2: Moving toward more biased codon usage in viral structural and nonstructural genes. J. Med. Virol. 92(6), 660-666 (2020).

    2. Lu, R., Zhao, X., Li, J., et alGenomic characterisation and epidemiology of 2019 novel coronavirus: Implications for virus origins and receptor binding. Lancet 395(10224), 565-574 (2020).

    3. Meo, S.A., Alhowikan, A.M., Al-Khlaiwi, T., et alNovel coronavirus 2019-nCoV: Prevalence, biological and clinical characteristics comparison with SARS-CoV and MERS-CoV. Eur. Rev. Med. Pharmacol. Sci. 24(4), 2012-2019 (2020).

    4. Klok, F.A., Kruip, M.J.H.A., van der Meer, N.J.M., et alIncidence of thrombotic complications in critically ill ICU patients with COVID-19. Thromb. Res. 191, 145-147 (2020).

    5. Yang, F., Shi, S., Zhu, J., et alAnalysis of 92 deceased patients with COVID-19. J. Med. Virol. 92(11), 2511-2515 (2020).

    6. Romano, M., Ruggiero, A., Squeglia, F., et alA structural view of SARS-CoV-2 RNA replication machinery: RNA synthesis, proofreading and final capping. Cells 9(5), 1267 (2020).

    7. Littler, D.R., Gully, B.S., Colson, R.N., et alCrystal structure of the SARS-CoV-2 non-structural protein 9, Nsp9. iScience 23(7), 101258 (2020).