Host: E. coli • AA: 1-198 • Tag: N-Terminal His and DYKDDK
Technical Support & Resources

Visit our FAQ

Contact Us

Toll Free Phone (USA and Canada Only): (888) 526-5351
Direct Phone: (734) 975-3888

Request Technical Support

Technical Support Request

To streamline the process attach the appropriate questionnaire to your inquiry.

Download IHC QuestionnaireDownload WB Questionnaire

View Our Privacy Statement for details on how we use and protect your data. In addition, this site is protected by hCaptcha and its Privacy Policy and Terms of Service apply.

SARS-CoV-2 nsp8 (recombinant)

Item No. 40882

Product Insert (PDF)
Technical Information
Synonyms
  • Severe Acute Respiratory Syndrome Coronavirus 2 nsp8
  • SARS-CoV-2 Non-structural Protein 8
Purity
≥90% estimated by SDS-PAGE
Endotoxin Testing
<1.0 EU/µg, determined by the LAL endotoxin assay
Source
Recombinant SARS-CoV-2 N-terminal His- and DYKDDK-tagged nsp8 expressed in E. coli
Amino Acids
1-198
Formulation (Request formulation change)
50 mM Tris-HCl, pH 7.5, with 200 mM sodium chloride and 20% glycerol
UniProt Accession №
P0DTD1
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
Recommended Products

Certificates of Analysis & Batch Specific Data

Provide batch numbers separated by commas to download or request available product inserts, QC sheets, certificates of analysis, data packs, and GC-MS data.

    100 µg

    $601

    Add

    500 µg

    $1,947

    Add
    Cayman Chemical
    Neutrophil Biology Wall Poster

    Explore how neutrophils shape the immune response in health and disease. This poster highlights neutrophil pathogen defense mechanisms, including phagocytosis, degranulation, and NETosis, as well as neutrophil roles in inflammation and NET-associated pathologies.

    DOWNLOAD NOW
    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 8 (nsp8) is encoded within ORF1ab and is a cofactor and component of the SARS-CoV-2 decameric RNA replication transcriptional complex. It functions as an anchoring scaffold for the RNA transcription complex, with its N-terminal domain (NTD) binding to the RNA-dependent polymerase (RdRp) nsp12, the helicase nsp13, and RNA.7 SARS-CoV-2 nsp8 also functions as a virulence factor, binding to the host 7SL RNA component of the signal recognition particle to suppress membrane protein trafficking and impair host antiviral responses.8

    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. Treviño, M.Á., Pantoja-Uceda, D., D.V., L., et al. SARS-CoV-2 Nsp8 N-terminal domain folds autonomously and binds dsRNA. Nucleic Acids Res. 51(18), 10041-10048 (2023).

    8. Banerjee, A.K., Blanco, M.R., Bruce, E.A., et al. SARS-CoV-2 disrupts splicing, translation, and protein trafficking to suppress host defenses. Cell 183(5), 1325-1339.e1321 (2020).