Host: Insect cells • AA: 686-1,213 • Tag: C-terminal mouse IgG1 Fc • MW: 84.33 kDa
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SARS-CoV-2 Spike Glycoprotein S2 Subunit (recombinant)

Item No. 31815

Technical Information
Synonyms
  • 2019-nCoV Surface Glycoprotein S2 Subunit
  • COVID-19 Spike Glycoprotein S2 Subunit
  • SARS-CoV-2 Spike Glycoprotein S2 Subunit
  • Severe Acute Respiratory Syndrome Coronavirus 2 Spike Glycoprotein S2 Subunit
Purity
≥95% estimated by SDS-PAGE
Endotoxin Testing
<1.0 EU/g determined by the LAL endotoxin assay
Source
Recombinant C-terminal mouse IgG1 Fc-tagged SARS-CoV-2 surface glycoprotein S2 subunit expressed in insect cells
Amino Acids
686-1,213
MW
84.3 kDa
Lyophilized from sterile 20 mM Tris, pH 7.0, 300 mM sodium chloride, and 100 mM glycine
Host
Insect cells
UniProt Accession №
P0DTC2
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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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 a viral structural protein encoded by the S gene in SARS-CoV-2 RNA.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 C-terminal S2 subunit, which facilitates fusion between viral and host cell membranes, contains a fusion peptide (FP) and two heptad repeats (HRs), as well as transmembrane and cytoplasmic domains.7,8 Upon insertion of the FP in the target cell membrane, the HRs form a six-helical bundle (6-HB) that enables SARS-CoV-2 to fuse with the target cell. The SARS-CoV-2 spike glycoprotein S2 subunit increases amyloid-β (1-40) (Aβ40) and Aβ42 levels in primary mouse neuron culture supernatants and the number of hippocampal and cortical Aβ plaques in APPswe/PSEN1dE9 transgenic mice.9 Cayman's SARS-CoV-2 Spike Glycoprotein S2 Subunit (recombinant) protein is a disulfide-linked homodimer. The reduced monomer, composed of the SARS-CoV-2 spike glycoprotein S2 subunit (amino acids 686-1,213) fused to mouse IgG1 Fc at its C-terminus, consists of 762 amino acids and has a calculated molecular weight of 84.3 kDa.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Kandeel, M., Ibrahim, A., Fayez, M., et alFrom 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 alGenomic 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 alNovel 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 alIncidence 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 alAnalysis of 92 deceased patients with COVID-19. J. Med. Virol. 92(11), 2511-2515 (2020).

    6. Liu, Z., Xiao, X., Wei, X., et alComposition 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 alStructure, function, and antigenicity of the SARS-CoV-2 spike glycoprotein. Cell 181(2), 281-292 (2020).

    8. Huang, Y., Yang, C., Xu, X.-F., et alStructural and functional properties of SARS-CoV-2 spike protein: Potential antivirus drug development for COVID-19. Acta Pharmacol. Sin. 41(9), 1141-1149 (2020).

    9. Ma, G., Zhang, D.-F., Zou, Q.-C., et alSARS-CoV-2 Spike protein S2 subunit modulates γ-secretase and enhances amyloid-β production in COVID-19 neuropathy. Cell Discov. 8(1), 99 (2022).