For inhibition of the spike glycoprotein RBD and ACE2 interaction
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SARS-CoV-2 Spike Glycoprotein Neutralizing Rabbit Monoclonal Antibody (Clone 001)

Item No. 31803

Product Insert (PDF)
Technical Information
Synonyms
  • SARS-CoV-2 Spike RBD
  • SARS-CoV-2 Spike Receptor Binding Domain
  • SARS-CoV-2 Surface Glycoprotein RBD
  • SARS-CoV-2 Surface Glycoprotein Receptor Binding Domain
  • Severe Acute Respiratory Syndrome Coronavirus 2 Spike Glycoprotein Receptor Binding Domain
  • Severe Acute Respiratory Syndrome Coronavirus 2 Surface Glycoprotein Receptor Binding Domain
Immunogen
Recombinant SARS-CoV-2 spike glycoprotein RBD (C-terminal mouse IgG1 Fc-tagged)
Clone Designation
001
100 µg of protein A-affinity purified monoclonal antibody
Storage Buffer
0.2 μm filtered solution in histidine and arginine with 120 mM sodium chloride, 0.02% Tween 80, and pH 6.0
Host
Rabbit
Isotype
IgG
Applications
ELISA, FC, MN assays
Cross Reactivity
(+) SARS-CoV-2 (BA.2.75) spike glycoprotein S1+S2 trimer(+) SARS-CoV-2 Delta (B.1.617.2) spike glycoprotein S1+S2 trimer(+) SARS-CoV-2 Delta (B.1.617.2) spike glycoprotein S1 subunit(+) SARS-CoV-2 spike glycoprotein S1 subunit(-) SARS-CoV-2 Omicron (BA.1.1) spike glycoprotein S1+S2 trimer(-) SARS-CoV-2 Omicron (B.1.1.529) spike glycoprotein S1 subunit(-) SARS-CoV-2 Omicron (B.1.1.529) S1+S2 trimer(-) SARS-CoV-2 Omicron (BA.2) spike glycoprotein S1+S2 trimer(-) SARS-CoV-2 Omicron (BA.2) spike glycoprotein S1 subunit(-) SARS-CoV-2 Omicron (BA.2) spike glycoprotein S1 subunit NTD(-) SARS-CoV-2 Omicron (BA.2.75.2) spike glycoprotein S1+S2 trimer(-) SARS-CoV-2 XD (BA.1 x AY.4) spike glycoprotein S1+S2 trimer(-) SARS-CoV-2 (BA.4.6) spike glycoprotein S1+S2 trimer(-) SARS-CoV-2 Omicron (BF.7) spike glycoprotein S1+S2 trimer(-) SARS-CoV-2 Omicron (BQ.1.1) spike glycoprotein S1+S2 trimer(-) SARS-CoV-2 Delta (B.1.617.2) spike glycoprotein S1 subunit NTD(-) SARS-CoV spike glycoprotein S1 subunit(-) 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 (BA.2.75)(+) SARS-CoV-2 (BA.2.3.20)(-) SARS-CoV-2 Omicron (BA.1.1)(-) SARS-CoV-2 Omicron (BA.1.1.529)(-) SARS-CoV-2 Omicron (BA.2)(-) SARS-CoV-2 Omicron (BA.2.12.1)(-) SARS-CoV-2 Omicron (BA.2.75.2)(-) SARS-CoV-2 Omicron (BA.4)(-) SARS-CoV-2 Omicron (BA.4.6/BF.7)(-) SARS-CoV-2 Omicron (BA.5)(-) SARS-CoV-2 Omicron (BQ.1.1)(-) SARS-CoV-2 Omicron (XBB)
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 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. 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.11,12 Cayman’s SARS-CoV-2 Spike Glycoprotein Neutralizing Rabbit Monoclonal Antibody (Clone 001) disrupts the spike glycoprotein S1 subunit-ACE2 interaction and can be used for ELISA, and flow cytometry (FC) 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 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. Hoffmann, M., Kleine-Weber, H., Schroeder, S., et alSARS-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 alStructural 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 alCryo-EM structure of the 2019-nCov spike in the prefusion conformation. Science 367(6483), 1260-1263 (2020).

    11. Wang, A., Zhang, L., Sang, L., et alKinetics of viral load and antibody response in relation to COVID-19 severity. J. Clin. Invest. 130(10), 5235-5244 (2020).

    12. Xiang, F., Wang, X., He, X., et alAntibody detection and dynamic characteristics in patients with coronavirus disease 2019. Clin. Infect. Dis. 71(8), 1930-1934 (2020).