For immunochemical detection of the SARS-CoV-2 surface glycoprotein
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SARS-CoV-2 Surface Glycoprotein Rabbit Monoclonal Neutralizing Antibody (Clone 004)

Item No. 33627

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Synonyms
  • 2019-nCoV Spike Glycoprotein
  • 2019-nCoV Surface Glycoprotein
  • COVID-19 Spike Glycoprotein
  • COVID-19 Surface Glycoprotein
  • SARS-CoV-2 Spike Glycoprotein
  • Severe Acute Respiratory Syndrome Coronavirus 2 Surface Glycoprotein
Immunogen
Recombinant SARS-CoV-2 Surface Glycoprotein RBD-mFc Protein
Clone Designation
004
Formulation (Request formulation change)
100 µg of protein A-purified monoclonal antibody
Storage Buffer
0.2 µm filtered solution in PBS
Host
HEK293 cells
Isotype
IgG
Applications
ELISA
Species Reactivity
(+) SARS-CoV-2(+) HCoV-HKU1 (isolate N1)(-) SARS-CoV(-) MERS-CoV(-) HCoV-HKU1 (isolate N5)(-) HCoV-NL63(-) HCoV-229E(-) HCoV-OC4
Shipping & Storage Information
Storage
-20°C
Shipping
Wet ice in continental US; may vary elsewhere
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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

    $605

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    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.

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    Product Description

    Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is an enveloped positive-stranded RNA virus, a member of the Betacoronavirus genus, and the causative agent of COVID-19.1,2,3,4,5 The SARS-CoV-2 surface glycoprotein, also known as the spike glycoprotein, is located on the outer envelope of the virion.1 It is composed of an S1 and S2 subunit divided by a furin S-cleavage site not found in other SARS-CoVs.6,7 The S1 subunit contains the receptor-binding domain (RBD), which binds to the carboxypeptidase angiotensin-converting enzyme 2 (ACE2), and the S1 and S2 subunits are cleaved by the protease TMPRSS2 to facilitate viral fusion with the host cell membrane.8,9,10 In this way, ACE2 acts as the functional receptor for SARS-CoV-2. SARS-CoV-2 infection can result in the production of neutralizing antibodies, which bind to the SARS-CoV-2 spike RBD preventing further viral entry and infection, starting approximately 4-10 days after symptom onset.11,12 Cayman’s SARS-CoV-2 Surface Glycoprotein Rabbit Monoclonal Neutralizing Antibody (Clone 004) disrupts the S1-RBD-ACE2 interaction and can be used for ELISA.

    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. Liu, Z., Xiao, X., Wei, X., et al. Composition and divergence of coronavirus spike proteins and host ACE2 receptors predict potential intermediate hosts of SARS-CoV-2. J. Med. Virol. 92(6), 595-601 (2020).

    7. Walls, A.C., Park, Y.-J., Tortorici, M.A., et al. Structure, function, and antigenicity of the SARS-CoV-2 spike glycoprotein. Cell 181(2), 281-292 (2020).

    8. Hoffmann, M., Kleine-Weber, H., Schroeder, S., et al. SARS-CoV-2 cell entry depends on ACE2 and TMPRSS2 and is blocked by a clinically proven protease inhibitor. Cell 181(2), 271-280 (2020).

    9. Yan, R., Zhang, Y., Li, Y., et al. Structural basis for the recognition of the SARS-CoV-2 by full-length human ACE2. Science 267(6485), 1444-1448 (2020).

    10. Wrapp, D., Wang, N., Corbett, K.S., et al. Cryo-EM structure of the 2019-nCov spike in the prefusion conformation. Science 367(6483), 1260-1263 (2020).

    11. Wang, A., Zhang, L., Sang, L., et al. Kinetics of viral load and antibody response in relation to COVID-19 severity. J. Clin. Invest. 130(10), 5235-5244 (2020).

    12. Xiang, F., Wang, X., He, X., et al. Antibody detection and dynamic characteristics in patients with coronavirus disease 2019. Clin. Infect. Dis. 71(8), 1930-1934 (2020).