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COVID-19 assays and reagents

3D medical animation corona virus

Scientists worldwide are facing new challenges to rapidly identify or develop treatments and vaccines against COVID-19.

Unravelling cellular factors involved in SARS-CoV-2 cellular entry as well as deciphering biological mechanisms aimed at protecting patients, are needed to reduce viral outbreak and reveal therapeutic targets.

As a distributor of specialty reagents and physiologically relevant in vitro assays, we are actively in contact with our manufacturers to bring you their validated products for research in relation to COVID-19. Our aim is to provide the European research community with tools to assist the collective effort towards accelerating the understanding of SARS-CoV-2 transmission, and to determine therapeutic strategies in the early stages of R&D projects.

Our teams are mobilized (either home-working or at our offices in accordance with local rules and recommendations), to assist and advise you in the choice, delivery and use of your reagents.


About SARS-CoV-2

SARS-CoV is composed of a helical nucleocapsid formed by its RNA genome interacting with nucleocapsid (N) proteins. This nucleocapsid is surrounded by a capsid and an envelope, formed by the structural proteins E, M, S and lipids.

The spike (S) protein of SARS-CoV belongs to a group of class I viral fusion protein,1 which facilitates viral entry into target cells. Entry depends on binding of the surface unit, S1, of the S protein to a cellular receptor, which facilitates viral attachment to the surface of target cells. In addition, entry requires S protein priming by cellular proteases, which entails S protein cleavage at the S1/S2 and the S2’ site and allows fusion of viral and cellular membranes2.

Protein N has been associated with multiple functions in SARS-CoV. First, it associates with the viral RNA during the assembly of the virion and allows the packaging of the genome inside of it.  In addition, the nucleocapsid protein would be involved in the modulation of different cellular signaling pathways by regulating the expression of certain actors in these pathways such as ERK, MAPK or JNK6. These changes include induction of apoptosis as well as reorganization of the cytoskeleton3.

Protein E is the main component of the viral envelope. It has a highly hydrophobic structure and this characteristic could allow it to modify the permeability of the infected cell by forming pores on the plasma membrane.

The matrix protein (protein M) is similar to that found in other coronaviruses, it plays a role in the assembly of the virus. It is the most abundant protein found on the surface of virions.

Research demonstrates that SARS-CoV-2 uses the SARS-CoV receptor ACE2 for entry and the serine protease TMPRSS2 for S protein priming. SARS-S engages angiotensin-converting enzyme 2 (ACE2) as the entry receptor 4 and employs the cellular serine protease TMPRSS2 for S protein priming5,6,7 The SARS-S/ACE2 interface has been elucidated at the atomic level, and the efficiency of ACE2 usage was found to be a key determinant of SARS-CoV transmissibility8.

A novel route involving CD147 (also known as Basigin (BSG) or extracellular matrix metalloproteinase inducer (EMMPRIN)) and SARS Spike (S) protein has been discovered9, opening new opportunities for the development of specific antiviral drugs targeted CD147 (e.g. Meplazumab for SARS-CoV-2 pneumonia)10.


To easily access the full range of corresponding reagents, simply type COVID-19 in our search engine from anywhere on our website.


COVID-19 (SARS-CoV-2) Variants research reagents and related products

Have you already tested your compounds against SARS-CoV-2, but you now need to verify their efficacy against the new Variants? 

COVID-19 (SARS-CoV-2) research reagents and related products

We have identified this selection of the most recent and relevant products in for COVID-19 research.

Lateral flow EIA Test Kits, ELISAs, and Arrays

  • COVID-19 IgG/IgM Rapid Test (Serum/Plasma/Whole Blood)
  • SARS-CoV-2 Human IgG (4-Plex): First planar-based multiplex assay to allow simultaneous detection of human IgG to the SARS-CoV-2 S1 protein, SARS-CoV-2 S2 protein, a negative control (Sheep Fc), and a positive control (anti-human IgG) from 2µl of blood sample.

Validated antibodies

Recombinant Proteins


Cell Lines

Cell Labelling

Pseudotyped lentivirus

Functional Assays & Compounds


RNA Purification & PCR

Supporting Reagents


  1. Du L, et al. "The spike protein of SARS-CoV — a target for vaccine and therapeutic development" Nat. Rev. Microbiol. (2009) March; 7(3): 226–236. doi:10.1038/nrmicro2090.
  2. Hoffmann, M. et al. "SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor" (2020) Cell. doi:10.1016/j.cell.2020.02.052.
  3. Surjit, M. et al. "The SARS coronavirus nucleocapsid protein induces actin reorganization and apoptosis in COS-1 cells in the absence of growth factors" (2004) Biochem. J. 383: 1–6. doi: 10.1042/BJ20040984
  4. Li et al. "Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus" (2003) Nature vol. 426, pages 450–454doi.org/10.1038/nature02145
  5. Glowacka et al. "Evidence that TMPRSS2 activates the severe acute respiratory syndrome coronavirus spike protein for membrane fusion and reduces viral control by the humoral immune response" (2011). doi: 10.1128/JVI.02232-10 
  6. Matsuyama et al. "Efficient activation of the severe acute respiratory syndrome coronavirus spike protein by the transmembrane protease TMPRSS2" (2010) J. VIROL., Vol. 84, No. 24, doi: 10.1128/JVI.01542-10
  7. Shulla et al. "A transmembrane serine protease is linked to the severe acute respiratory syndrome coronavirus receptor and activates virus entry" (2011) J. VIROL., Vol. 85, No. 2, doi: 10.1128/JVI.02062-10
  8. Li et al. "Structure of SARS coronavirus spike receptor-binding domain complexed with receptor" (2005) Science, Vol. 309, Issue 5742, doi: 10.1126/science.1116480
  9. Wang K. et al. "SARS-CoV-2 invades host cells via a novel route: CD147-spike protein" (2020) , bioRxiv, doi: doi.org/10.1101/2020.03.14.988345
  10. Huijie B. et al. "Meplazumab treats COVID-19 pneumonia: an open-labelled, concurrent controlled add-on clinical trial" (2020) medRxiv, doi.org/10.1101/2020.03.21.2004069
  11. Qiao et al, . " Targeting transcriptional regulation of SARS-CoV-2 entry factors ACE2 and TMPRSS2 " PNAS January 5, 2021 118 (1). doi.org/10.1073/pnas.2021450118