SARS-CoV-2 nsp14 Antibody - BSA Free

Immunohistochemistry: SARS-CoV-2 nsp14 Antibody [NBP3-07053] - Immunohistochemical analysis of paraffin-embedded COVID-19 patient lung tissue using anti- SARS-CoV-2 (COVID-19) NSP14 antibody (0.5 ug/mL). Tissue was fixed with formaldehyde and blocked with 10% serum for 1 h at RT; antigen retrieval was by heat mediation with a citrate buffer (pH6). Samples were incubated with primary antibody overnight at 4 degrees celsius. A goat anti-rabbit IgG H&L (HRP) at 1/250 was used as secondary. Counter stained with Hematoxylin. Strong signal of SARS-COV-2 NSP14 protein was observed in macrophage of COVID-19 patient lung, but not in non-COVID-19 patient lung.

• Reactivity: V
• Applications: ELISA, IHC
• Clonality: Polyclonal
• Host: Rabbit
• Conjugate: Unconjugated
• Format: BSA Free
• Concentration: 1 mg/ml

SARS-CoV-2 nsp14 Antibody - BSA Free Summary

• Immunogen: This antibody was raised against a peptide corresponding to 14 amino acids near the center of SARS-CoV-2 (COVID-19) NSP14 (ExoN) protein. The immunogen is located between 120-170 amino acids of SARS-CoV-2 (COVID-19) NSP14 (ExoN).
• Isotype: IgG
• Clonality: Polyclonal
• Host: Rabbit
• Gene: ORF1ab
• Purity: Peptide affinity purified

Applications/Dilutions

• Dilutions:
  • ELISA 1 ug/mL
  • Immunohistochemistry 0.5 ug/mL

Packaging, Storage & Formulations

• Storage: Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.
• Buffer: PBS
• Preservative: 0.02% Sodium Azide
• Concentration: 1 mg/ml
• Purity: Peptide affinity purified

Alternate Names for SARS-CoV-2 nsp14 Antibody - BSA Free

• ExoN
• Guanine-N7 methyltransferase
• Non-structural protein 14
• nsp14
• Proofreading exoribonuclease

Background

SARS-CoV-2 Nonstructural Protein 14 (NSP14) is one of the sixteen nonstructural proteins of severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2), the causative agent of COVID-19 (1). SARS-CoV-2 NSP14 is 527 amino acids (aa) with a theoretical molecular weight of 59.8 kDa (1-3). The amino acid sequence alignment of SARS-CoV and SARS-CoV-2's NSP14 has 95.1% sequence identity and 99.1% sequence similarity (1). Functionally, NSP14 has both 3'-5' exoribonuclease activity and N7-methyltransferase activity (1-4). The N-terminal domain of NSP14 has exoribonuclease activity (ExoN) with three conserved motifs (DE, E, and D) and belongs to the DEDD superfamily (3,4). NSP14 ExoN activity has a role in RNA proofreading during viral replication (3,4). NSP10 has been shown to interact with the exoribonuclease domain of NSP14, increasing its activity (3,4). On the other hand, the carboxyl-terminal of NSP14 has the N7-methyltransferase activity and functions in viral mRNA capping (3,4).

References

1. Yoshimoto F. K. (2020). The Proteins of Severe Acute Respiratory Syndrome Coronavirus-2 (SARS CoV-2 or n-COV19), the Cause of COVID-19. The Protein Journal. https://doi.org/10.1007/s10930-020-09901-4

2. Gordon, D. E., Jang, G. M., Bouhaddou, M., Xu, J., Obernier, K., White, K. M., O'Meara, M. J., Rezelj, V. V., Guo, J. Z., Swaney, D. L., Tummino, T. A., Huttenhain, R., Kaake, R. M., Richards, A. L., Tutuncuoglu, B., Foussard, H., Batra, J., Haas, K., Modak, M., Kim, M., ... Krogan, N. J. (2020). A SARS-CoV-2 protein interaction map reveals targets for drug repurposing. Nature. https://doi.org/10.1038/s41586-020-2286-9

3. Qiu, Y., & Xu, K. (2020). Functional studies of the coronavirus nonstructural proteins. STEMedicine. https://doi.org/10.37175/stemedicine.v1i2.39

4. Romano, M., Ruggiero, A., Squeglia, F., Maga, G., & Berisio, R. (2020). A Structural View of SARS-CoV-2 RNA Replication Machinery: RNA Synthesis, Proofreading and Final Capping. Cells. https://doi.org/10.3390/cells9051267

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

Bioinformatics

• Gene Symbol: ORF1ab