Active • Host: HEK293 cells • Tag: C-terminal mouse IgG1 Fc • AA: 16-685 • MW: 101.4 kDa
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SARS-CoV-2 Spike Glycoprotein S1 Subunit (recombinant)

Item No. 31814

Product Insert (PDF)Safety Data Sheet (SDS) (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
Purity
≥90% estimated by SDS-PAGE
Endotoxin Testing
<1.0 EU/µg, determined by the LAL endotoxin assay
Source
Active recombinant C-terminal mouse IgG1 Fc-tagged SARS-CoV-2 surface glycoprotein S1 subunit expressed in HEK293 cells
Amino Acids
16-685
MW
101.4 kDa
Formulation (Request formulation change)
Lyophilized from sterile PBS, pH 7.4
UniProt Accession №
P0DTC2
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    100 µg

    $543

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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 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 (recombinant) can be used for ELISA. This protein is a disulfide-linked homodimer. The reduced monomer, composed of the SARS-CoV-2 spike glycoprotein S1 subunit (amino acids 16-685) fused to mouse IgG1 Fc at its C-terminus, consists of 904 amino acids and has a calculated molecular weight of 101.4 kDa. As a result of glycosylation, the monomer migrates at approximately 116 kDa by SDS-PAGE under reducing conditions.

    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).