SARS-CoV-2 nsp14 Antibody [DyLight 350] 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 |
Innovator's Reward |
Test in a species/application not listed above to receive a full credit towards a future purchase. |
Applications/Dilutions
Dilutions |
- ELISA
- Immunohistochemistry
|
Application Notes |
Optimal dilution of this antibody should be experimentally determined. |
Reactivity Notes
Packaging, Storage & Formulations
Storage |
Store at 4C in the dark. |
Buffer |
50mM Sodium Borate |
Preservative |
0.05% Sodium Azide |
Purity |
Peptide affinity purified |
Notes
DyLight (R) is a trademark of Thermo Fisher Scientific Inc. and its subsidiaries.
Alternate Names for SARS-CoV-2 nsp14 Antibody [DyLight 350]
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.
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