SARS-CoV-2 Nucleocapsid MAb (Clone 1035111)

Catalog # Availability Size / Price Qty
MAB10474-100
MAB10474-SP
Detection of SARS-CoV-2 Nucleocapsid by Western Blot.
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Citations (9)
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SARS-CoV-2 Nucleocapsid MAb (Clone 1035111) Summary

Species Reactivity
SARS-CoV-2
Specificity
Detects SARS-CoV-2 Nucleocapsid in direct ELISAs and Western blots. No cross-reactivity with MERS Nucleocapsid is observed in Western blots.
Source
Monoclonal Mouse IgG2B Clone # 1035111
Purification
Protein A or G purified from hybridoma culture supernatant
Immunogen
Spodoptera frugiperda, Sf 21-derived SARS-CoV-2 Nucleocapsid protein
Met1-Ala419
Accession # YP_009724397.2
Formulation
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS.
Label
Unconjugated

Applications

Recommended Concentration
Sample
Western Blot
2 µg/mL
Recombinant SARS-CoV-2 Nucleocapsid protein
Immunohistochemistry
5-25 µg/mL
Immersion fixed paraffin-embedded sections of SARS-CoV-2 infected human lung

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Scientific Data

Western Blot Detection of SARS-CoV-2 Nucleocapsid antibody by Western Blot. View Larger

Detection of SARS-CoV-2 Nucleocapsid by Western Blot. Western blot shows recombinant SARS-CoV-2 Nucleocapsid protein. PVDF membrane was probed with 2 µg/mL of Mouse Anti-SARS-CoV-2 Nucleocapsid Monoclonal Antibody (Catalog # MAB10474) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (HAF018). A specific band was detected for SARS-CoV-2 Nucleocapsid at approximately 50 kDa (as indicated). This experiment was conducted under reducing conditions and using Western Blot Buffer Group 1.

Immunohistochemistry View Larger

SARS-CoV-2 Nucleocapsid in SARS-CoV-2 Infected Human Lung. SARS-CoV-2 Nucleocapsid was detected in immersion fixed paraffin-embedded sections of SARS-CoV-2 infected human lung (left, positive staining) and normal human lung (right, negative control) using Mouse Anti-SARS-CoV-2 Nucleocapsid Monoclonal Antibody (Catalog # MAB10474) at 5 µg/mL for 1 hour at room temperature followed by incubation with the Anti-Mouse IgG VisUCyte™ HRP Polymer Antibody (VC001). Before incubation with the primary antibody, tissue was subjected to heat-induced epitope retrieval using Antigen Retrieval Reagent-Basic (CTS013). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue). Specific staining was localized to SARS-CoV-2 infected cells. Staining was performed using our protocol for IHC Staining with VisUCyte HRP Polymer Detection Reagents.

Reconstitution Calculator

Reconstitution Calculator

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Preparation and Storage

Reconstitution
Reconstitute at 0.5 mg/mL in sterile PBS.
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Shipping
Lyophilized product is shipped at ambient temperature. Liquid small pack size (-SP) is shipped with polar packs. Upon receipt, store immediately at the temperature recommended below.
Stability & 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.
  • 6 months, -20 to -70 °C under sterile conditions after reconstitution.

Background: Nucleocapsid

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).

References
  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.
Long Name
Nucleocapsid Protein
Entrez Gene IDs
918763 (HCoV-229E); 3200423 (HCoV-HKU1); 2943504 (HCoV-NL63); 39105221 (HCoV-OC43); 14254601 (MERS-CoV); 1489678 (SARS-CoV); 43740575 (SARS-CoV-2)
Alternate Names
N Protein; Nucleocapsid protein; Nucleocapsid; ORF9a protein

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Citations for SARS-CoV-2 Nucleocapsid MAb (Clone 1035111)

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

9 Citations: Showing 1 - 9
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  1. Virological characteristics of a SARS-CoV-2-related bat coronavirus, BANAL-20-236
    Authors: Fujita, S;Plianchaisuk, A;Deguchi, S;Ito, H;Nao, N;Wang, L;Nasser, H;Tamura, T;Kimura, I;Kashima, Y;Suzuki, R;Suzuki, S;Kida, I;Tsuda, M;Oda, Y;Hashimoto, R;Watanabe, Y;Uriu, K;Yamasoba, D;Guo, Z;Hinay, AA;Kosugi, Y;Chen, L;Pan, L;Kaku, Y;Chu, H;Donati, F;Temmam, S;Eloit, M;Yamamoto, Y;Nagamoto, T;Asakura, H;Nagashima, M;Sadamasu, K;Yoshimura, K;Suzuki, Y;Genotype to Phenotype Japan (G2P-Japan) Consortium, ;Ito, J;Ikeda, T;Tanaka, S;Matsuno, K;Fukuhara, T;Takayama, K;Sato, K;
    EBioMedicine
    Species: Hamster - Mesocricetus auratus (Golden Hamster)
    Sample Types: Whole Tissue
    Applications: Immunohistochemistry
  2. Human Post-Translational SUMOylation Modification of SARS-CoV-2 Nucleocapsid Protein Enhances Its Interaction Affinity with Itself and Plays a Critical Role in Its Nuclear Translocation
    Authors: Madahar, V;Dang, R;Zhang, Q;Liu, C;Rodgers, VGJ;Liao, J;
    Viruses
    Species: Human
    Sample Types: Cell Lysates
    Applications: Western Blot
  3. Virological characteristics of the SARS-CoV-2 XBB variant derived from recombination of two Omicron subvariants
    Authors: Tamura, T;Ito, J;Uriu, K;Zahradnik, J;Kida, I;Anraku, Y;Nasser, H;Shofa, M;Oda, Y;Lytras, S;Nao, N;Itakura, Y;Deguchi, S;Suzuki, R;Wang, L;Begum, MM;Kita, S;Yajima, H;Sasaki, J;Sasaki-Tabata, K;Shimizu, R;Tsuda, M;Kosugi, Y;Fujita, S;Pan, L;Sauter, D;Yoshimatsu, K;Suzuki, S;Asakura, H;Nagashima, M;Sadamasu, K;Yoshimura, K;Yamamoto, Y;Nagamoto, T;Schreiber, G;Maenaka, K;Genotype to Phenotype Japan (G2P-Japan) Consortium, ;Hashiguchi, T;Ikeda, T;Fukuhara, T;Saito, A;Tanaka, S;Matsuno, K;Takayama, K;Sato, K;
    Nature communications
    Species: Syrian Hamster
    Sample Types: Whole Tissue
    Applications: IHC
  4. Convergent evolution of SARS-CoV-2 Omicron subvariants leading to the emergence of BQ.1.1 variant
    Authors: Ito, J;Suzuki, R;Uriu, K;Itakura, Y;Zahradnik, J;Kimura, KT;Deguchi, S;Wang, L;Lytras, S;Tamura, T;Kida, I;Nasser, H;Shofa, M;Begum, MM;Tsuda, M;Oda, Y;Suzuki, T;Sasaki, J;Sasaki-Tabata, K;Fujita, S;Yoshimatsu, K;Ito, H;Nao, N;Asakura, H;Nagashima, M;Sadamasu, K;Yoshimura, K;Yamamoto, Y;Nagamoto, T;Kuramochi, J;Schreiber, G;Genotype to Phenotype Japan (G2P-Japan) Consortium, ;Saito, A;Matsuno, K;Takayama, K;Hashiguchi, T;Tanaka, S;Fukuhara, T;Ikeda, T;Sato, K;
    Nature communications
    Species: Hamster
    Sample Types: Whole Tissue
    Applications: IHC
  5. Human antibody recognition and neutralization mode on the NTD and RBD domains of SARS-CoV-2 spike protein
    Authors: R Otsubo, T Minamitani, K Kobiyama, J Fujita, T Ito, S Ueno, I Anzai, H Tanino, H Aoyama, Y Matsuura, K Namba, KI Imadome, KJ Ishii, K Tsumoto, W Kamitani, T Yasui
    Scientific Reports, 2022-11-22;12(1):20120.
    Species: Hamster
    Sample Types: Whole Tissue
    Applications: IHC
  6. Structure-based dual affinity optimization of a SARS-CoV-1/2 cross-reactive single-domain antibody
    Authors: T Sulea, J Baardsnes, M Stuible, N Rohani, A Tran, M Parat, Y Cepero Don, M Duchesne, P Plante, G Kour, Y Durocher
    PLoS ONE, 2022-03-30;17(3):e0266250.
    Species: Human
    Sample Types: Whole Cells
    Applications: Neutralization
  7. Attenuated fusogenicity and pathogenicity of SARS-CoV-2 Omicron variant
    Authors: R Suzuki, D Yamasoba, I Kimura, L Wang, M Kishimoto, J Ito, Y Morioka, N Nao, H Nasser, K Uriu, Y Kosugi, M Tsuda, Y Orba, M Sasaki, R Shimizu, R Kawabata, K Yoshimatsu, H Asakura, M Nagashima, K Sadamasu, K Yoshimura, Genotype t, H Sawa, T Ikeda, T Irie, K Matsuno, S Tanaka, T Fukuhara, K Sato
    Nature, 2022-02-01;0(0):.
    Species: Hamster
    Sample Types: Whole Tissue
    Applications: IHC
  8. Enhanced fusogenicity and pathogenicity of SARS-CoV-2 Delta P681R mutation
    Authors: A Saito, T Irie, R Suzuki, T Maemura, H Nasser, K Uriu, Y Kosugi, K Shirakawa, K Sadamasu, I Kimura, J Ito, J Wu, K Iwatsuki-H, M Ito, S Yamayoshi, S Loeber, M Tsuda, L Wang, S Ozono, EP Butlertana, YL Tanaka, R Shimizu, K Shimizu, K Yoshimatsu, R Kawabata, T Sakaguchi, K Tokunaga, I Yoshida, H Asakura, M Nagashima, Y Kazuma, R Nomura, Y Horisawa, K Yoshimura, A Takaori-Ko, M Imai, Genotype t, S Tanaka, S Nakagawa, T Ikeda, T Fukuhara, Y Kawaoka, K Sato
    Nature, 2021-11-25;0(0):.
    Species: Hamster
    Sample Types: Whole Tissue
    Applications: IHC
  9. Lingering SARS-CoV-2 in Gastric and Gallbladder Tissues of Patients with Previous COVID-19 Infection Undergoing Bariatric Surgery
    Authors: Mohamed Hany, Ahmed Zidan, Muhammad Gaballa, Mohamed Ibrahim, Ann Samy Shafiq Agayby, Anwar Ashraf Abouelnasr et al.
    Obesity Surgery

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