Proteins for Coronavirus Research

Proteins for Coronavirus Research

COVID-19 research and drug development speed along at an unprecedented pace as the scientific community searches for a cure. At R&D Systems, we understand the importance of quality recombinant proteins and enzymes with documented bioactivity and consistent performance for studying SARS-CoV-2 and other coronaviruses. We offer a range of different Spike proteins, as well as bioactive Papain-like proteases and 3CL proteases. With over 95% purity, the SARS-CoV-2 Nucleocapsid protein is an ideal antigen. Trusted for over 35 years, R&D Systems is the leading provider of recombinant proteins to the life science community.

Coronavirus Proteins

R&D Systems offers a range of SARS-CoV-2 proteins and other Coronavirus proteins with the same industry-leading quality specifications as our other recombinant proteins. Our SARS-CoV-2 Spike proteins exhibit high affinity binding to human ACE-2 in both ELISA and SPR. And the Coronavirus proteases, Papain-like Protease and 3CL protease, are tested for bioactivity using biologically relevant fluorescent substrates. For more detailed information about our recombinant Coronvirus proteins, visit the product pages listed below.

NEW Application Note: Glycosylation of the receptor binding domain of COVID-19 virus spike protein

Coronavirus Proteins

SARS-CoV-2 Proteins

Protein Species Source Tag Catalog # Bioactivity
SARS-CoV-2 Spike Protein RBD SARS-CoV-2 HEK293 Fc 10499-CV Binds ACE-2 (Catalog # 933-ZN)
CHO Fc 10542-CV
Sf21 Fc 10565-CV
Please Inquire
HEK293 His 10500-CV
CHO His 10534-CV
Tn5 His 10523-CV
SARS-CoV-2 Spike (Active Trimer) SARS-CoV-2 HEK293 His 10549-CV Binds ACE-2 (Catalog # 933-ZN)
SARS-CoV-2 Spike (GCN4-IZ) SARS-CoV-2 HEK293 His 10561-CV Binds ACE-2 (Catalog # 933-ZN)
SARS-CoV-2 Spike S1 Subunit Protein SARS-CoV-2 HEK293 His 10569-CV Binds ACE-2 (Catalog # 933-ZN)
Sf21 His 10522-CV
SARS-CoV-2 Spike S2 Subunit SARS-CoV-2 Tn5 His 10584-CV
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SARS-CoV-2 Nucleocapsid Protein SARS-CoV-2 Sf21 His 10474-CV Bioactivity not tested, >95% pure by SDS-PAGE
SARS-CoV-2 Papain-like Protease SARS-CoV-2 E. coli No tag E-611 Cleaves Ubiquitin-Rhodamine 110 (Catalog # U-555)
SARS-CoV-2 3CL Protease SARS-CoV-2 E. coli No tag E-720 Cleaves SARS CoV-2 3CL Protease Substrate, Rh110-conjugated (Catalog # S-720)

SARS CoV Proteins

Protein Species Source Tag Catalog # Bioactivity
SARS-CoV Spike RBD Protein SARS-CoV CHO His 10558-CV Binds ACE-2 (Catalog # 933-ZN)
CHO Fc 10559-CV
HEK293 His 10583-CV
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HEK293 Fc 10582-CV
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SARS-CoV Spike S1 Subunit Protein SARS-CoV Sf21 His 10570-CV Binds ACE-2 (Catalog # 933-ZN)
SARS-CoV Spike (GCN4-IZ) SARS-CoV CHO His 10581-CV
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SARS Virus Papain-like Protease SARS-CoV E. coli No tag E-610 Cleaves Ubiquitin-Rhodamine 110 (Catalog # U-555)
SARS-CoV 3CL Protease SARS-CoV E. coli No tag E-718 Cleaves SARS CoV-2 3CL Protease Substrate, Rh110-conjugated (Catalog # S-720)

MERS and other Coronavirus Proteins

Protein Species Source Tag Catalog # Bioactivity
MERS-CoV Nucleocapsid Protein MERS-CoV Sf21 His 10521-CV N/A
MERS-CoV Papain-like Protease MERS-CoV E. coli His E-609 Cleaves Ubiquitin-Rhodamine 110 (Catalog # U-555)
MERS-CoV 3CL Protease MERS-CoV E. coli No tag E-719
Please Inquire
 
Bat CoV Spike RBD Protein Bat CoV CHO Fc 10556-CV Binds mouse ACE-2 (Catalog # 3437-ZN)

Receptor recognition

Coronavirus binding to a cell surface receptor is a key mechanism of infection and a major focus of therapeutic research. Using proteins that are bioactive and have the correct conformation is critical for binding and drug development studies. Every protein listed below is QC tested for bioactivity and lot-to-lot consistency.

ACE-2 Receptor Recognition

Protein Species Source Tag Catalog # Bioactivity
ACE-2 Human NS0 His 933-ZN Binds SARS-CoV-2 S Protein RBD (10499-CV)
Mouse CHO His 3437-ZN Cleaves the fluorogenic peptide substrate, Mca-YVADAPK(Dnp)-OH (Catalog # ES007)
Rat NS0 His 4516-ZN
Human CHO Fc 10544-ZN Binds SARS-CoV-2 S Protein RBD (10499-CV)
Pig HEK293 His 10545-ZN Cleaves the fluorogenic peptide substrate, Mca-YVADAPK(Dnp)-OH (Catalog # ES007
Canine HEK293 His 10566-ZN Cleaves the fluorogenic peptide substrate, Mca-YVADAPK(Dnp)-OH (Catalog # ES007)
DPPIV Human NS0 His 9168-SE Cleaves the fluorogenic peptide substrate, Gly-Pro-7-amido-4-methylcoumarin (GP-AMC)
Mouse NS0 His 954-SE
Cyno HEK293 His 9637-SE
Aminopeptidase N/CD13 Human NS0 His 3815-ZN Cleaves the fluorogenic peptide substrate, Ala-7-amido-4-methylcoumarin (Ala-AMC)
Mouse NS0 His 2335-ZN
CEACAM-1 Human NS0 His 2244-CM Inhibits IL-2 secretion by T cells
LY6E Human HEK293 Fc 9970-L6 Inhibits IFN-gamma and IL-2 secretion by T cells
EMMPRIN/CD147 Human NS0 Fc, His 972-EMN Induces active MMP-1 secretion by NHLF human normal lung fibroblasts
Mouse NS0 His 772-EM
Neuropilin-1 Human NS0 His 3870-N1 Binds VEGF 165
Mouse Sf21 His 5994-N1

Proteases

Host cell proteases are involved in coronavirus protein processing and activation. All enzymes listed are bioactive and QC tested to ensure consistency and activity.

Protein Species Source Tag Catalog # Bioactivity
Cathepsin B Human NS0 His 953-CY Cleaves the fluorogenic peptide substrate Z-LR-AMC (Catalog # ES008)
Mouse NS0 His 965-CY
Cathepsin L Human NS0 His 952-CY Cleaves the fluorogenic peptide substrate Z-LR-AMC (Catalog # ES008)
Mouse NS0 His 1515-CY
Furin Human NS0 His 1503-SE Cleaves the fluorogenic peptide substrate pERTKR-AMC (Catalog # ES013)
Mouse CHO His 6450-SE
Elastase/ELA2 Human CHO His 9167-SE Cleaves the fluorogenic peptide substrate, MeOSuc-Ala-Ala-Pro-Val-7-amido-4-methylcoumarin (MeOSuc-AAPV-AMC
Mouse NS0 His 4517-SE

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About Coronavirus Proteins

Spike Protein

The Coronavirus Spike protein (S Protein) is one of four major structural proteins covering the surface of each virion. The Spike protein is a highly glycosylated, type I transmembrane protein responsible for host cell entry. Structurally, there are two domains, S1 and S2, that play major roles in receptor binding and membrane fusion. Within the N-terminal S1 domain is the receptor binding domain (Spike RBD protein). The Spike RBD binds to the host cell and initiates viral infection. The SARS-CoV-2 Spike RBD tightly associates with human ACE-2. Once the Spike S1 domain binds to its host receptor, conformational changes occur in the Spike S2 domain allowing for membrane attachment and eventually transfer of the nucleocapsid into the cell. Because of its essential role during Coronavirus infection, the Spike protein is major therapeutic target.

Nucleocapsid Protein

The Coronavirus Nucleocapsid protein (N Protein) is a multifunctional RNA-binding protein required for viral RNA transcription, replication, and packaging. The Nucleocapsid protein consists of three domains, an N-terminal RNA-binding domain, a central intrinsically disordered region, followed by a C-terminal dimerization domain. The RNA-binding domain contains multiple positively charged binding surfaces that form charged interactions with RNA promoting its helical arrangement. The Nucleocapsid protein is highly antigenic making it an attractive target for vaccine development and serological assays.

Papain-like Protease

The Coronavirus Papain-like protease (PLPro) is one of several nonstructural proteins (nsps) and along with 3CL Protease, is responsible for processing of viral proteins into functional, mature subunits during maturation. For example, PLPro cleaves a site at the amino-terminal end of the viral replicase region. In addition to its role in viral protein maturation, Papain-like protease exhibits both a deubiquitinating and deISG15ylating activity. In vivo, this protease antagonizes innate immunity by acting on IFN beta and NF- kappa B signaling pathways. Purified PLPro is used in vitro with polyubiquitin substrates demonstrating a strong preference for K48 linkages.

3CL Protease

The Coronavirus 3CL protease (3CLpro) is the other main protease in addition to the Papain-like protease and is required for processing of viral polypeptides into distinct, functional proteins. The SARS-CoV-2 3CL Protease is a C30-type cysteine protease located within the non-structural proteins 3 (NS3) region of the viral polypeptide. Analysis of the Coronavirus genome reveals at least 11 sites of cleavage for the 3CL Protease, many containing the amino acid sequence LQ[S/A/G]. In addition to the Papain-Like Protease, 3CLpro presents a promising therapeutic target for COVID-19. One attractive advantage of 3CLpro is that no human proteases are known to have a similar cleavage specificity making inhibitors of 3CLpro unlikely to cause mechanism-based toxicity.