Proteins for Coronavirus Research

Proteins for Coronavirus Research

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

Spike Protein

Protein   Source Tag Catalog # Bioactivity
SARS-CoV-2 Spike Protein RBD  Spike 2 HEK293 Fc 10499-CV Binds ACE-2 (Catalog # 933-ZN)
CHO Fc 10542-CV
Sf21 Fc 10565-CV
HEK293 His 10500-CV
CHO His 10534-CV
Tn5 His 10523-CV
SARS-CoV-2 Spike Protein RBD, Biotinylated Spike 2 HEK293 His BT10500 Binds ACE-2 (Catalog # 10544-ZN)
HEK293 Avi-tag, Fc AVI10499, Please Inquire  
SARS-CoV-2 Spike (Active Trimer) S2 HEK293 His 10549-CV Binds ACE-2 (Catalog # 933-ZN)
CHO His 10586-CV
SARS-CoV-2 D614G Spike, Active Trimer S2 HEK293 His 10587-CV Binds ACE-2 (Catalog # 933-ZN)
SARS-CoV-2 Spike Protein, biotinylated S2 HEK293 His BT10549 Please Inquire  
SARS-CoV-2 Spike (GCN4-IZ) S2 HEK293 His 10561-CV Binds ACE-2 (Catalog # 933-ZN)
SARS-CoV-2 Spike S1 Subunit Protein S2 HEK293 His 10569-CV Binds ACE-2 (Catalog # 933-ZN)
Sf21 His 10522-CV
SARS-CoV-2 D614G Spike S1 Subunit S2 HEK293 His 10609-CV
Please Inquire
 
SARS-CoV-2 Spike S1 Subunit Protein, Biotinylated S2 HEK293 His BT10569
Please Inquire
 
SARS-CoV-2 Spike S2 Subunit S2 Tn5 His 10584-CV  
SARS-CoV-2 Spike S2 Subunit (GCN4-IZ) S2 HEK293 His 10590-CV Please Inquire  
SARS-CoV Spike RBD Protein Spike 2 CHO His 10558-CV Binds ACE-2 (Catalog # 933-ZN)
CHO Fc 10559-CV
HEK293 His 10583-CV
HEK293 Fc 10582-CV
SARS-CoV Spike S1 Subunit Protein S2 Sf21 His 10570-CV Binds ACE-2 (Catalog # 933-ZN)
SARS-CoV Spike (GCN4-IZ) S2 CHO His 10581-CV Binds ACE-2 (Catalog # 933-ZN)
MERS-CoV Spike S1 Subunit Protein S2 CHO Fc 10606-CV  
HCoV-NL63 Spike S1 Subunit Protein Spike 2 HEK293 His 10605-CV, Please Inquire  
HCoV-HKU1 Spike S1 Subunit Protein Spike 2 HEK293 His 10600-CV, Please Inquire  
HCoV-229E Spike RBD Protein Spike 2 HEK293 His 10612-CV
Please Inquire
 
Bat CoV Spike RBD Protein Spike 2 CHO Fc 10556-CV Binds mouse ACE-2 (Catalog # 3437-ZN)
CHO His 10593-CV Binds human ACE-2 (Catalog # 10544-ZN)

Spike Protein Data

ELISA

Recombinant Human ACE-2

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Recombinant SARS-CoV-2 Spike S1 Subunit His-tag (Catalog # 10569-CV) binds Recombinant Human ACE-2 (933-ZN) in a functional ELISA.

SDS-PAGE

SDS page

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2 µg/lane of Recombinant SARS-CoV-2 Spike (Active Trimer) His Protein (10549-CV) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 144-175 kDa.

SPR

Surface Plasmon Resonance

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Binding of ACE-2 to SARS-CoV-2 Spike RBD by surface plasmon resonance (SPR). Recombinant SARS-CoV-2 Spike RBD His-tag Protein (Catalog # 10523-CV) was immobilized on a Biacore Sensor Chip CM5, and binding to recombinant human ACE-2 (Catalog # 933-ZN) was measured at a concentration range between 0.37 nM and 93.5 nM. The double-referenced sensorgram was fit to a 1:1 binding model to determine the binding kinetics and affinity, with an affinity constant of KD=1.910 nM. (Biacore T200).

SEC

Recombinant SARS-CoV-2 Spike Proteins

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Recombinant SARS-CoV-2-Spike Proteins, Active Trimmer(Catalog # 10549-CV) was analyzed by size exclusion chromatography (SEC) resulting in a single major peak. The predicted MW was calculated to be 373kDa, consisted with a trimeric conformation.

Nucleocapsid Protein

Protein   Source Tag Catalog # Bioactivity
SARS-CoV-2 Nucleocapsid Protein S2 Sf21 His 10474-CV Bioactivity not tested, >95% pure by SDS-PAGE
MERS-CoV Nucleocapsid Protein S2 Sf21 His 10521-CV Bioactivity not tested, >95% pure by SDS-PAGE

Coronavirus Proteases

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)
CHO Fc 10544-ZN
Mouse CHO His 3437-ZN Cleaves the fluorogenic peptide substrate, Mca-YVADAPK(Dnp)-OH (Catalog # ES007)
Rat NS0 His 4516-ZN
Pig HEK293 His 10545-ZN
Hamster HEK293 His 10578-ZN Binds SARS-CoV-2 S Protein RBD (10499-CV)
ACE-2, Biotinylated Human CHO Avi-tag, His AVI10579 Binds SARS-CoV-2 S Protein RBD (10499-CV)
CHO Avi-tag, Fc AVI10544
HEK293 Avi-tag, His Please Inquire
HEK293 Avi-tag, Fc Please Inquire
NS0 His BT933
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

Host Cell 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

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.

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.