Recombinant MERS-CoV Spike S1 Subunit Fc Chimera Protein, CF Summary
For a complete list of Spike Proteins and other Coronavirus proteins
Measured by its binding ability in a functional ELISA with Recombinant Human DPPIV/CD26 (High Purity Dimer) (Catalog # 9168-SE).
|MERS-CoV Spike S1 Subunit|
Accession # K9N5Q8.1
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.|
|Reconstitution||Reconstitute at 500 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
Recombinant MERS-CoV Spike S1 Subunit Fc Chimera (Catalog # 10606-CV) binds Recombinant Human DPPIV/CD26 (High Purity Dimer) (9168-SE) in a functional ELISA.
2 μg/lane of Recombinant MERS-CoV Spike S1 Subunit Fc Chimera (Catalog # 10606-CV) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 115-135 kDa and 220-260 kDa, respectively.
In a functional flow cytometry test, (A) Recombinant MERS-CoV Spike S1 Subunit Fc chimera Protein (Catalog # 10606-CV) binds to HEK293 human embryonic kidney cell line transfected with recombinant human CD26/DPPIV and EGFP. Ligand binding was detected by staining cells with APC-conjugated anti-Human IgG Fc Monoclonal Antibody (FAB110A), which does not stain the cells in the absence of recombinant protein (B).
Background: Spike S1 Subunit
MERS-CoV (also known as HCoV-EMC), which causes the Middle East Respiratory Syndrome (MERS), belongs to a family of viruses known as coronaviruses that are commonly comprised of a large plus-strand RNA genome and four structural proteins: Spike protein (S), Envelope protein (E), Membrane protein (M), and Nucleocapsid protein (N) (1,2). Other well-known human coronaviruses include several viruses that cause relatively mild respiratory disease, plus two viruses that caused the Severe Acute Respiratory Syndrome (SARS-CoV) and the global pandemic Covid-19 (SARS-CoV2). MERS-CoV Spike Protein (S Protein) is a glycoprotein that mediates membrane fusion and viral entry, and it consists of two subunits, S1 and S2. The S1 subunit is focused on attachment of the protein to the host receptor while the S2 subunit is involved with cell fusion (3). Based on amino acid (aa) sequence homology, the MERS-CoV S1 subunit shares 23% and 22% identity with SARS-CoV S1 subunit and SARS-Cov2 S1 subunit, respectively. The low aa sequence homology is consistent with the finding that MERS-CoV and SARS-CoV bind different cellular receptors (4). Unlike SARS-CoV and SARS-CoV2, which engage ACE2 as their receptors for cell entry, MERS-CoV employs Dipeptidyl Peptidase 4 (DPP4; also known as CD26) as its functional receptor (4). Based on structural biology studies, the receptor binding domain (RBD) of MERS-CoV spike protein is located in the C-terminal region of S1 subunit and consists of a core subdomain and a receptor-binding subdomain (5, 6). The S1 subunit, especially the RBD region, was commonly targeted for vaccinations or antiviral therapy against MERS (7-9).
- Bermingham, A. et al. (2012) Euro Surveill. 17:20290.
- Zaki, A.M. et al. (2012) N. Engl. J. Med. 367:1814.
- Li, Y. et al. (2019) Engineering. 5:940.
- Raj, V.S. et al. (2013) Nature 495:251.
- Lu, G. et al. (2013) Nature 500:227.
- Wang, N. et al. (2013) Cell. Res. 23:986.
- Corti, D. et al. (2016) J. Infect. Public Health 9:231.
- Tang, X.C. et al. (2014) Proc. Natl. Acad. Sci. USA 111:E2018.
- Jiang, L. et al. (2014) Sci. Transl. Med. 6:234ra59.
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