Active • Host: E. coli • AA: 1-306 of MERS-CoV Mpro (full length), 3,248-3,553 of K9N638 • MW: 33.33 kDa
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MERS-CoV Mpro (recombinant)

Item No. 40987

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Synonyms
  • 3CLpro
  • 3C-like Protease
  • Main Protease
  • nsp5
Purity
≥85%
Source
Active recombinant MERS-CoV Mpro expressed in E. coli
Amino Acids
1-306 of MERS-CoV Mpro (full length), 3,248-3,553 of K9N638
MW
33.33 kDa
Formulation (Request formulation change)
20 mM HEPES, pH 7.5, 10% glycerol, 150 mM sodium chloride, 1 mM TCEP, and 1 mM EDTA
Applications
Enzyme assays
UniProt Accession №
K9N638
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    100 µg

    $439

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    Cayman Chemical
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    Product Description

    Middle East respiratory syndrome coronavirus (MERS-CoV) is an enveloped positive-stranded RNA virus, a member of the Betacoronavirus genus, and the causative agent of MERS, an acute respiratory disease that often leads to pneumonia and renal failure.1,2 The MERS-CoV main protease (Mpro), also known as 3C-like protease (3CLpro), is encoded by non-structural protein 5 (nsp5), exists as a homodimer, and is composed of a chymotrypsin-like catalytic domain and helical domain.3,4 It is involved in processing polyprotein 1a (pp1a) at positions 4-16, which produces 13 nsps, and in inhibiting the host antiviral innate immune response.3,5,6 Inhibition of MERS-CoV Mpro activity reduces MERS-CoV replication in infected cells in vitro.7 MERS-CoV Mpro inhibition also increases survival and decreases lung viral titers and edema in MERS-CoV-infected transgenic mice expressing the gene encoding human dipeptidyl peptidase 4 (DPP-4), which is the functional receptor of MERS-CoV.7,8 Cayman’s MERS-CoV Mpro (recombinant) protein can be used for enzyme activity assays. MERS-CoV Mpro activity reflects its concentration-dependent dimerization (Kd = ~7-8 µM), an intrinsic property of the enzyme.9

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Du, L., Yang, Y., Zhou, Y., et al. MERS-CoV spike protein: A key target for antivirals. Expert Opin. Ther. Targets 21(2), 131-143 (2017).

    2. Rabaan, A.A., Al-Ahmed, S.H., Haque, S., et al. SARS-CoV-2, SARS-CoV, and MERS-CoV: A comparative overview. Infez. Med. 28(2), 174-184 (2020).

    3. Li, Y.-H., Hu, C.-Y., Wu, N.-P., et al. Molecular characteristics, functions, and related pathogenicity of MERS-CoV proteins. Engineering (Beijing) 5(5), 940-947 (2019).

    4. Ho, B.-L., Cheng, S.-C., Shi, L., et al. Critical assessment of the important residues involved in the dimerization and catalysis of MERS coronavirus main protease. PLoS One 10(12), e0144865 (2015).

    5. Zhang, Y., Kandwal, S., Fayne, D., et al. MERS-CoV-nsp5 expression in human epithelial BEAS 2b cells attenuates type I interferon production by inhibiting IRF3 nuclear translocation. Cell. Mol. Life Sci. 81(1), 433 (2024).

    6. van Huizen, M. The Main protease of Middle East Respiratory Syndrome Coronavirus induces cleavage of mitochondrial antiviral signaling protein to antagonize the innate immune response. Viruses 16(2), 256 (2024).

    7. Rathnayake, A.D., Zheng, J., Kim, Y., et al. 3C-like protease inhibitors block coronavirus replication in vitro and improve survival in MERS-CoV-infected mice. Sci. Transl. Med. 12(557), eabc5332 (2020).

    8. Du, H., Wang, D.W., and Chen, C. The potential effects of DPP-4 inhibitors on cardiovascular system in COVID-19 patients. J. Cell. Mol. Med. 24(18), 10274-10278 (2020).

    9. Tomar, S., Johnston, M.L., St. John, S.E., et al. Ligand-induced dimerization of Middle East respiratory syndrome (MERS) coronavirus nsp5 protease (3CLpro): Implications for nsp5 regulation and the development of antivirals. The Journal of Biological Chemisty 290(32), 19403-19422 (2015).