Active • Host: E. coli • AA: 5325-5925 • MW: 69.1 kDa
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SARS-CoV-2 nsp13 Helicase (E. coli expressed)

Item No. 30589

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Synonyms
  • 2019-nCOV Helicase
  • COVID-19 Helicase
  • NSP13
  • SARS-CoV-2 Helicase, COVID19 Helicase
  • Severe Acute Respiratory Syndrome Coronavirus 2 nsp13 Helicase
Purity
≥70% estimated by SDS-PAGE
Source
Active recombinant N-terminal His-tagged nsp13 helicase expressed in E. coli
Amino Acids
5,325-5,925
MW
69.1 kDa
Formulation (Request formulation change)
50 mM Tris-HCl, pH 7.5, with 5 µM zinc chloride, 1 mM DTT, 1 mM EDTA, and 15% glycerol
UniProt Accession №
P0DTD1
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    10 µg

    $369

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    Cayman Chemical
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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 nsp13 helicase is a superfamily 1B helicase and component of replicase polyprotein 1a (PP1a), which is encoded by ORF1a in the viral genome. It is composed of two canonical RecA-like ATPase domains, 1A and 2A, and a zinc-binding domain, stalk region, and 1B domain.7,8 SARS-CoV-2 nsp13 functions as both an RNA helicase and a nucleoside triphosphate hydrolase (NTPase), unwinding RNA in an NTP-dependent manner.9 It inhibits IFN-β reporter gene activation induced by the RIG-I 2CARD domain in 293FT cells, indicating a role for nsp13 helicase in suppression of the host immune response.10 Cayman's SARS-CoV-2 nsp13 Helicase (E. coli expressed) protein can be used for enzyme assays and Western blot (WB) applications.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Kandeel, M., Ibrahim, A., Fayez, M., et al. From 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 al. Genomic 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 al. Novel 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 al. Incidence 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 al. Analysis of 92 deceased patients with COVID-19. J. Med. Virol. 92(11), 2511-2515 (2020).

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

    7. Chen, J., Malone, B., Llewellyn, E., et al. Structural basis for helicase-polymerase coupling in the SARS-CoV-2 replication-transcription complex. Cell (2020).

    8. Mirza, M.U., and Froeyen, M. Structural elucidation of SARS-CoV-2 vital proteins: Computational methods reveal potential drug candidates against main protease, Nsp12 polymerase and Nsp13 helicase. J. Pharm. Anal. (2020).

    9. Shu, T., Huang, M., Wu, D., et al. SARS-Coronavirus-2 Nsp13 possesses NTPase and RNA helicase activities that can be inhibited by bismuth salts. Virol. Sin. 35(3), 321-329 (2020).

    10. Yuen, C.-K., Lam, J.-Y., Wong, W.-M., et al. SARS-CoV-2 nsp13, nsp14, nsp15 and orf6 function as potent interferon antagonists. Emerg. Microbes Infect. 9(1), 1418-1428 (2020).