For immunochemical detection of the SARS-CoV-2 spike glycoprotein S1 subunit
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SARS-CoV-2 Spike Glycoprotein S1 Subunit Polyclonal Antibody

Item No. 32502

Product Insert (PDF)
Technical Information
Synonyms
  • COVID-19 Surface Glycoprotein S1 Subunit
  • 2019-nCoV Surface Glycoprotein S1 Subunit
  • SARS-CoV-2 Surface Glycoprotein S1 Subunit
  • Severe Acute Respiratory Syndrome Coronavirus 2 Spike Glycoprotein S1 Subunit
Immunogen
Recombinant SARS-CoV-2 spike glycoprotein S1 subunit (C-terminal His-tagged)
Formulation (Request formulation change)
50 or 100 µl of antigen-affinity purified polyclonal antibody
Storage Buffer
0.2 μm filtered solution in PBS
Host
Rabbit
Isotype
IgG
Applications
ELISA, WB
Cross Reactivity
(+) SARS-CoV-2 spike glycoprotein RBD (mouse Fc-tagged)(+) SARS-CoV spike glycoprotein S1 subunit (His-tagged)(+) SARS-CoV spike glycoprotein RBD (His-tagged)
Species Reactivity
(+) SARS-CoV-2(+) SARS-CoV
Shipping & Storage Information
Storage
-80°C
Shipping
Dry 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.

    50 µl

    $149

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    100 µl

    $253

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    Cayman Chemical
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    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 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 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 Cayman’s SARS-CoV-2 Spike Glycoprotein S1 Subunit Polyclonal Antibody can be used for ELISA and Western blot (WB) applications. The antibody recognizes the spike glycoprotein S1 subunit from SARS-CoV-2 and SARS-CoV.

    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).