Recombinant MERS-CoV Spike S1 (GCN4-IZ) His-tag Protein, CF

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Recombinant MERS-CoV Spike S1 Subunit (GCN4-IZ) His-tag (Catalog # 10737-CV) binds Recombinant Human DPPIV/CD26 (High Purity Dimer) (9168-SE) in a functional ELISA.
2 μg/lane of Recombinant MERS-CoV Spike S1 (GCN4-IZ) His-tag (Catalog # 10737-CV) was resolved with SDS-PAGE under reducing (R) conditions and visualized by Coomassie® Blue staining, showing bands at 105-125 kDa.

Product Details

Summary
Reactivity VSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant MERS-CoV Spike S1 (GCN4-IZ) His-tag Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA with Recombinant Human DPPIV/CD26 (High Purity Dimer) (Catalog # 9168-SE).
Source
Human embryonic kidney cell, HEK293-derived mers-cov Spike S1 Subunit protein
MERS-CoV Spike S1 Subunit
(Tyr18-Pro747)
Accession # YP_007188579.1
GCN4-IZ6-His tag
N-terminusC-terminus
Accession #
N-terminal Sequence
Tyr18
Protein/Peptide Type
Recombinant Proteins
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
86 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
105-125 kDa, under reducing conditions

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 500 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant MERS-CoV Spike S1 (GCN4-IZ) His-tag Protein, CF

  • SARS-CoV-2
  • Spike S1 Subunit

Background

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).
  1. Bermingham, A. et al. (2012) Euro Surveill. 17:20290.
  2. Zaki, A.M. et al. (2012) N. Engl. J. Med. 367:1814.
  3. Li, Y. et al. (2019) Engineering. 5:940.
  4. Raj, V.S. et al. (2013) Nature 495:251.
  5. Lu, G. et al. (2013) Nature 500:227.
  6. Wang, N. et al. (2013) Cell. Res. 23:986.
  7. Corti, D. et al. (2016) J. Infect. Public Health 9:231.
  8. Tang, X.C. et al. (2014) Proc. Natl. Acad. Sci. USA 111:E2018.
  9. Jiang, L. et al. (2014) Sci. Transl. Med. 6:234ra59.

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