Recombinant SARS-CoV-2 Nucleocapsid His Protein, CF

2 μg/lane of Recombinant SARS-CoV-2 Nucleocapsid His Protein (Catalog # 10474-CV) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 44-53 kDa.

• Reactivity: V
• Format: Carrier-Free

Recombinant SARS-CoV-2 Nucleocapsid His Protein, CF Summary

• Additional Information: Sf21 Insect Cell Expressed, Over 95% Purity
• Details of Functionality: Bioassay data are not available.
• Source: Spodoptera frugiperda, Sf 21 (baculovirus)-derived sars-cov-2 Nucleocapsid protein
  Met1-Ala419, with a C-terminal 6-His tag
• Accession #: YP_009724397.2
• N-terminal Sequence: Ser2
• Protein/Peptide Type: Recombinant Proteins
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity not tested
• Theoretical MW: 46 kDa.
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
• SDS-PAGE: 44-53 kDa, under reducing conditions

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS.
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 500 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant SARS-CoV-2 Nucleocapsid His Protein, CF

• N Protein
• Nucleocapsid protein
• Nucleocapsid
• ORF9a protein

Background

SARS-CoV-2, which causes the global pandemic coronavirus disease 2019 (Covid-19), belongs to a family of viruses known as coronaviruses that are commonly comprised of four structural proteins: Spike protein (S), Envelope protein (E), Membrane protein (M), and Nucleocapsid protein (N) (1).  While the S, E and M proteins build up the viral envelop, the N protein is involved transcription, replication and packaging of the viral RNA genome into a helical ribonucleocapsid (RNP) (2, 3).  The SARS-CoV-2 N protein is a ~45 kDa protein composed of two independent structural domains connected by a linker region. The N-terminal region contains an RNA binding domain, the linker region interacts with the M protein and the C-terminal region contains a self-association domain (2,3). The SARS-CoV2 N protein shares 91% and 47% amino acid sequence identity with SARS-CoV-1 and MERS N protein, respectively.  The SARS-CoV-2 N protein displays VSR (viral suppressor of RNA interference) activity in mammalian cells (4). In addition, the N protein is an abundant protein during coronavirus infection and displays high immunogenic activity (5, 6), so it has been used to develop serological diagnostic kit for Covid-19 IgM and IgG antibody tests (7).

1. Wu, F. et al. (2020) Nature 579:265.
2. Chang, C. K. et al. (2006) J. Biomed. Sci. 13:59.
3. Hurst, K. R. et al. (2009) J. Virol. 83:7221.
4. Mu, J. et al. (2020) Sci. China Life Sci. doi: 10.1007/s11427-020-1692-1.
5. Che, X. Y. et al. (2004) J. Clin. Microbiol. 42:2629.
6. Guan, M. et al. (2004) Clin. Diagn. Lab. Immunol. 11:287.
7. Liu, W. et al. (2020) J. Clin. Microbiol. doi: 10.1128/JCM.00461-20.

Publications for Nucleocapsid (10474-CV)(6)

Publications using 10474-CV

• Haystead, T;Lee, E;Cho, K;Gullickson, G;Hughes, P;Krafsur, G;Freeze, R;Scarneo, S; Investigation of SARS-CoV-2 individual proteins reveals the in vitro and in vivo immunogenicity of membrane protein Scientific reports 2023-12-18 [PMID: 38129491] (Bioassay, Human)
• Kiszel, P;Sík, P;Miklós, J;Kajdácsi, E;Sinkovits, G;Cervenak, L;Prohászka, Z; Class switch towards spike protein-specific IgG4 antibodies after SARS-CoV-2 mRNA vaccination depends on prior infection history Scientific reports 2023-08-13 [PMID: 37574522] (ELISA Capture, Human)
• ML Berre, T Paulov?áko, CM Verissimo, S Doyle, JP Dalton, C Masterson, ER Martínez, L Walsh, C Gormley, JG Laffey, B McNicholas, AJ Simpkin, M Kilcoyne A new multiplex SARS-CoV-2 antigen microarray showed correlation of IgG, IgA, and IgM antibodies from patients with COVID-19 disease severity and maintenance of relative IgA and IgM antigen binding over time PLoS ONE, 2023;18(3):e0283537. 2023 [PMID: 36996259] (Binding, Human)
• ML Berre, T Paulov?áko, CM Verissimo, S Doyle, JP Dalton, C Masterson, ER Martínez, L Walsh, C Gormley, JG Laffey, B McNicholas, AJ Simpkin, M Kilcoyne A new multiplex SARS-CoV-2 antigen microarray showed correlation of IgG, IgA, and IgM antibodies from patients with COVID-19 disease severity and maintenance of relative IgA and IgM antigen binding over time PLoS ONE, 2023-03-30;18(3):e0283537. 2023-03-30 [PMID: 36996259] (Binding, Human)
• G Sinkovits, J Schnur, L Hurler, P Kiszel, ZZ Prohászka, P Sík, E Kajdácsi, L Cervenak, V Maráczi, M Dávid, B Zsigmond, É Rimanóczy, C Bereczki, L Willems, EJM Toonen, Z Prohászka Evidence, detailed characterization and clinical context of complement activation in acute multisystem inflammatory syndrome in children Scientific Reports, 2022-11-17;12(1):19759. 2022-11-17 [PMID: 36396679] (ELISA Standard, Human)
• Y Kiyan, A Schultalbe, E Chernobriv, S Tkachuk, S Rong, N Shushakova, H Haller Calcium dobesilate reduces SARS-CoV-2 entry into endothelial cells by inhibiting virus binding to heparan sulfate Scientific Reports, 2022-10-07;12(1):16878. 2022-10-07 [PMID: 36207386] (Bioassay, Human)

Bioinformatics

• Uniprot:
  • YP_009724397.2()