For inhibition of the spike glycoprotein S1 subunit and ACE2 interaction
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SARS-CoV-2 Spike Glycoprotein S1 Subunit Neutralizing Monoclonal Antibody (Clone 43)

Item No. 31999

Product Insert (PDF)
Technical Information
Synonyms
  • SARS-CoV-2 Spike S1 Subunit
  • SARS-CoV-2 Surface Glycoprotein S1 Subunit
  • Severe Acute Respiratory Syndrome Coronavirus 2 Spike Glycoprotein S1 Subunit
  • Severe Acute Respiratory Syndrome Coronavirus 2 Surface Glycoprotein S1 Subunit
Immunogen
Recombinant SARS-CoV-2 spike glycoprotein S1 subunit (C-terminal mouse IgG1 Fc-tagged)
Clone Designation
43
Formulation (Request formulation change)
100 µg of protein A-affinity purified monoclonal antibody
Storage Buffer
0.2 μm filtered solution in PBS
Host
Mouse
Isotype
IgG1
Applications
ELISA, FC, IHC; P, MN assays
Cross Reactivity
(+) SARS-CoV-2 Delta (B.1.617.2) spike glycoprotein S1+S2 trimer(+) SARS-CoV-2 Delta (B.1.617.2) spike glycoprotein RBD(+) SARS-CoV-2 spike glycoprotein RBD(-) SARS-CoV-2 Omicron (BA.1.1) spike glycoprotein S1+S2 trimer(-) SARS-CoV-2 Omicron (BA.1.1) spike glycoprotein RBD(-) SARS-CoV-2 Omicron (B.1.1.529) S1+S2 trimer(-) SARS-CoV-2 Omicron (B.1.1.529) spike glycoprotein RBD(-) SARS-CoV-2 Omicron (BA.2) spike glycoprotein S1+S2 trimer(-) SARS-CoV-2 Omicron (BA.2) spike glycoprotein RBD(-) SARS-CoV-2 Omicron (BA.2) spike glycoprotein S1 subunit-NTD(-) SARS-CoV-2 Omicron (BA.2.12.1) spike glycoprotein RBD(-) SARS-CoV-2 Omicron (BA.4) spike glycoprotein RBD(-) SARS-CoV-2 Omicron (BA.5) spike glycoprotein RBD(-) SARS-CoV-2 XD (BA.1 x AY.4) spike glycoprotein S1+S2 trimer(-) SARS-CoV-2 Delta (B.1.617.2) spike glycoprotein S1 subunit-NTD(-) SARS-CoV-2 spike glycoprotein S1 subunit-NTD (C-terminal human IgG1 Fc- and AVI-tagged)(-) SARS-CoV spike glycoprotein S1 subunit (mouse Fc-tagged)(-) SARS-CoV spike glycoprotein RBD (His-tagged)(-) MERS-CoV spike glycoprotein S1 subunit(-) HCoV-HKU1 (isolate N1) spike glycoprotein S1 subunit(-) HCoV-HKU1 (isolate N5) spike glycoprotein S1 subunit(-) HCoV-NL63 spike glycoprotein S1 subunit(-) HCoV-229E spike glycoprotein S1 subunit(-) HCoV-OC43 spike glycoprotein S1+S2 ECD
Species Reactivity
(+) SARS-CoV-2(+) SARS-CoV-2 Delta (B.1.617.2)(-) SARS-CoV-2 Omicron (BA.2)
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    100 µg

    $549

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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, a member of the Betacoronavirus genus, and the causative agent of COVID-19.1,2,3,4,5 The SARS-CoV-2 spike glycoprotein, also known as the surface 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. The SARS-CoV-2 spike glycoprotein S1 subunit induces inflammatory gene expression in the frontal cortex, hippocampus, and hypothalamus, as well as activates toll-like receptor 2 (TLR2) and TLR4 signaling and increases social avoidance in the juvenile social exploration test in rats.11 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.12,13 Cayman’s SARS-CoV-2 Spike Glycoprotein S1 Subunit Neutralizing Monoclonal Antibody (Clone 43) disrupts the spike glycoprotein S1 subunit-ACE2 interaction and can be used for ELISA, flow cytometry (FC), and immunohistochemistry (IHC; paraffin) applications, as well as microneutralization (MN) assays.

    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. Frank, M.G., Ngyuen, K.H., Ball, J.B., et al. SARS-CoV-2 spike S1 subunit induces neuroinflammatory, microglial and behavioral sickness responses: Evidence of PAMP-like properties. Brain Behav. Immun. 100, 267-277 (2022).

    12. 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).

    13. 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).