SARS-CoV-2 Spike S1 Subunit Antibody Summary
Accession # YP_009724390.1
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Detection of SARS-CoV-2 Spike S1 by Western Blot. Western blot shows lysates of recombinant SARS-CoV-2 Spike S1 Subunit and recombinant SARS-CoV-2 Spike RBD. PVDF membrane was probed with 2 µg/mL of Mouse Anti-SARS-CoV-2 Spike S1 Monoclonal Antibody (Catalog # MAB105403) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (HAF018). A specific band was detected for Spike S1 at approximately 90 kDa (as indicated). This experiment was conducted under reducing conditions and using Western Blot Buffer Group 1.
Detection of SARS-CoV-2 Spike S1 protein bound to ACE-2 in live HEK293 Human Cell Line Transfected with Human ACE-2 and eGFP by Flow Cytometry. HEK293 human embryonic kidney cell line transfected with human ACE-2 and eGFP was incubated with Recombinant SARS-CoV-2 Spike S1 Subunit His-Tag protein (10522-CV), then stained with (A) Mouse Anti-SARS-CoV-2 Spike S1 Monoclonal Antibody (Catalog # MAB105403) or (B) Mouse IgG1 Isotype Control Antibody (MAB002) followed by Allophycocyanin-conjugated Anti-Mouse IgG Secondary Antibody (F0101B). Staining was performed using our Staining Membrane-associated Proteins protocol.
Detection of SARS-CoV-2 Spike S1 protein bound to ACE-2 in fixed HEK293 Human Cell Line Transfected with Human ACE-2 and eGFP by Flow Cytometry. HEK293 human embryonic kidney cell line transfected with human ACE-2 and eGFP was incubated with Recombinant SARS-CoV-2 Spike S1 Subunit His-Tag protein (10522-CV), then stained with (A) Mouse Anti-SARS-CoV-2 Spike S1 Monoclonal Antibody (Catalog # MAB105403) or (B) Mouse IgG1 Isotype Control Antibody (MAB002) followed by Allophycocyanin-conjugated Anti-Mouse IgG Secondary Antibody (F0101B). Prior to staining, cells were fixed with Flow Cytometry Fixation Buffer (FC004). Staining was performed using our Staining Membrane-associated Proteins protocol.
Spike S1 Subunit in SARS-CoV-2 Infected Human Lung. Spike S1 Subunit was detected in immersion fixed paraffin-embedded sections of SARS-CoV-2 infected human lung tissue using Mouse Anti-SARS-CoV-2 Spike S1 Monoclonal Antibody (Catalog # MAB105403) at 15 µg/mL for 1 hour at room temperature followed by incubation with the Anti-Mouse IgG VisUCyte™ HRP Polymer Antibody ( VC001). Before incubation with the primary antibody, tissue was subjected to heat-induced epitope retrieval using Antigen Retrieval Reagent-Basic (CTS013). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue). Specific staining was localized to SARS-CoV-2 infected cells. Staining was performed using our protocol for IHC Staining with VisUCyte HRP Polymer Detection Reagents.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: Spike S1 Subunit
SARS-CoV-2, which causes the global pandemic coronavirus disease 2019 (Covid-19), belongs to a family of viruses known as coronaviruses that are commonly comprised of four structural proteins: Spike protein(S), Envelope protein (E), Membrane protein (M), and Nucleocapsid protein (N) (1). SARS-CoV-2 Spike Protein (S Protein) is a glycoprotein that mediates membrane fusion and viral entry. The S protein is homotrimeric, with each ~180-kDa monomer consisting of two subunits, S1 and S2 (2). In SARS-CoV-2, as with most coronaviruses, proteolytic cleavage of the S protein into two distinct peptides, S1 and S2 subunits, is required for activation. The S1 subunit is focused on attachment of the protein to the host receptor while the S2 subunit is involved with cell fusion (3-5). Based on structural biology studies, the receptor binding domain (RBD), located in the C-terminal region of S1, can be oriented either in the up/standing or down/lying state (6). The standing state is associated with higher pathogenicity and both SARS-CoV-1 and MERS can access this state due to the flexibility in their respective RBDs. A similar two-state structure and flexibility is found in the SARS-CoV-2 RBD (7). Based on amino acid (aa) sequence homology, the SARS-CoV-2 S1 subunit has 65% identity with SARS-CoV-1 S1 subunit, but only 22% homology with the MERS S1 subunit. The low aa sequence homology is consistent with the finding that SARS and MERS bind different cellular receptors (8). The S Protein of the SARS-CoV-2 virus, like the SARS-CoV-1 counterpart, binds Angiotensin-Converting Enzyme 2 (ACE2), but with much higher affinity and faster binding kinetics (9). Before binding to the ACE2 receptor, structural analysis of the S1 trimer shows that only one of the three RBD domains in the trimeric structure is in the "up" conformation. This is an unstable and transient state that passes between trimeric subunits but is nevertheless an exposed state to be targeted for neutralizing antibody therapy (10). Polyclonal antibodies to the RBD of the SARS-CoV-2 S1 subunit have been shown to inhibit interaction with the ACE2 receptor, confirming RBD as an attractive target for vaccinations or antiviral therapy (11). There is also promising work showing that the RBD may be used to detect presence of neutralizing antibodies present in a patient's bloodstream, consistent with developed immunity after exposure to the SARS-CoV-2 virus (12). Lastly, it has been demonstrated the S Protein can invade host cells through the CD147/EMMPRIN receptor and mediate membrane fusion (13, 14).
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- Wang, X. et al. (2020) https://doi.org/10.1038/s41423-020-0424-9.
- Wang, K. et al. (2020) bioRxiv https://www.biorxiv.org/content/10.1101/2020.03.14.988345v1.
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