Active • Host: HEK293 cells • AA: 319-541 • Tag: C-terminal rabbit IgG1 Fc • MW: 50.3 kDa
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SARS-CoV-2 Spike Glycoprotein Receptor Binding Domain (rabbit IgG1 Fc-tagged)

Item No. 30590

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Synonyms
  • SARS-CoV-2 Spike Receptor Binding Domain
  • S1 RBD
  • Severe Acute Respiratory Syndrome Coronavirus 2 Spike Glycoprotein Receptor Binding Domain
  • Spike S1 RBD
Purity
≥85%
Source
Active recombinant C-terminal rabbit IgG1 Fc-tagged SARS-CoV-2 surface glycoprotein receptor binding domain expressed in HEK293 cells
Amino Acids
319-541
MW
50.3 kDa
Formulation (Request formulation change)
PBS, pH 7.4, with 5% mannitol, 5% trehalose, 0.01% Tween 20, and 10% glycerol
UniProt Accession №
P0DTC2
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    100 µg

    $623

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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. Cayman’s SARS-CoV-2 Spike Glycoprotein Receptor Binding Domain (rabbit IgG1 Fc-tagged) protein can used for ELISA, surface plasmon resonance (SPR), and Western blot (WB) applications.

    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).