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MERS Coronavirus Spike Glycoprotein (S1), His-Tag (E. coli)

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MERS Coronavirus Spike Glycoprotein (S1), His-tag is a recombinant protein containing a peptide from amino acids 56 to 295 of MERS-CoV Spike protein S1, cloned and expressed in E. coli, with

SDS-PAGE: Coomassie-stained SDS-PAGE showing purified recombinant MERS-CoV Spike (S1) protein.


MERS Coronavirus Spike Glycoprotein (S1), His-Tag is a recombinant protein, cloned and expressed in E. coli with



  • MERS Coronavirus Spike Glycoprotein (S1), His-Tag.
  • Recombinant protein manufactured in E. coli, with a 6xHis tag at its C-terminus (Accession: AHC74088).
  • Contains a peptide from amino acids 56 to 295 of Spike protein S1.
  • Purity >95% as determined by 10% PAGE (Coomassie staining).
  • For use in ELISA and other immunoassays.



Middle East respiratory syndrome (MERS), also known as camel flu, is a viral respiratory infection caused by the MERS-coronavirus (MERS-CoV). MERS-CoV is a betacoronavirus derived from bats. Since April 2012, cases of the Middle East Respiratory Syndrome Coronavirus (MERS-CoV) have been identified in middle east and other countries, causing severe illnesses with ~35% mortality.  Spread between humans typically requires close contact with an infected person. Camels have been shown to have antibodies to MERS-CoV but the exact source of infection in camels was not identified. Camels are also believed to be involved in transmission to humans. MERS-CoV genomes are phylogenetically classified into two clades, Clade A and B. Early cases of MERS were of Clade A clusters (EMC/2012 and Jordan-N3/2012), whilst more recent cases have been Clade B (Chu et al., 2014).

Three MERS-CoV proteins are expressed on the envelope of the virus: the surface spike protein (S), the membrane glycoprotein (M), and the envelope protein (E). The S protein is responsible for viral entry via attachment to and fusion with the host cell membrane. Spike protein has two domains, S1 and S2; the S1 domain is responsible for cellular tropism and interaction with target cell, whilst the S2 domain is responsible for membrane fusion. MERS-CoV has pandemic potential but there is currently no specific vaccine or treatment for the disease. However, the C terminus of S1 contains a receptor binding domain with potential for vaccine development and use in diagnostics (Xu et al., 2019). To this end, a peptide from amino acids 56 to 295 of spike protein S1 was expressed and purified from E. coli, with a 6 x His tag is attached to its C-terminus.



  • Chu et al. (2014). MERS Coronaviruses in Dromedary Camels, Egypt. Emerging Infectious Diseases. 20 (6): 1049–1053.
  • Xu et al. (2019). Antibodies and vaccines against Middle East respiratory syndrome coronavirus. Emerg Microbes Infect. 2019; 8(1): 841–856.

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