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Swine H1N1 Nucleocapsid Protein Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| IF, E |
|---|---|
| Primary Accession | C4AL25 |
| Other Accession | ACQ76305, 229535818 |
| Reactivity | Virus |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | IgG |
| Application Notes | NP antibody can be used for the detection of the NP protein from the H1N1 strain of swine-origin Influenza A in ELISA. For immunofluorescence start at 20 µg/mL. |
| Reconstitution & Storage | Swine H1N1 Nucleocapsid Protein antibody can be stored at 4℃ for three months and -20℃, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures. |
|---|---|
| Precautions | Swine H1N1 Nucleocapsid Protein Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Background
Swine H1N1 Nucleocapsid Protein Antibody: Influenza A virus is a major public health threat, killing more than 30, 000 people per year in the USA. In early 2009, a novel swine-origin influenza A (H1N1) virus (S-OIV) was identified in specimens obtained from patients in Mexico and the United States. The influenza A virus polymerase transcribes and replicates eight virion RNA (vRNA) segments, among which the nucleocapsid protein (NP), thought to control whether mRNA or cRNA is produced. The nucleoprotein (NP), which has multiple functions during the virus life cycle, possesses regions that are highly conserved among influenza A, B, and C viruses. It was recently found several NP mutations that affected the efficient incorporation of multiple viral-RNA (vRNA) segments into progeny virions even though a single vRNA segment was incorporated efficiently. This indicates that the respective conserved amino acids in NP may be critical for the assembly and/or incorporation of sets of eight vRNA segments.
References
Thompson WW, Shay DK, Weintraub, et al. Mortality associated with influenza and respiratory syncytial virus in the United States. JAMA2003; 289:179-186.
Novel Swine-Origin Influenza A (H1N1) Virus Investigation Team, Dawood FS, Jain S, et al. Emergence of a novel swine-origin influenza A (H1N1) virus in humans. N. Engl. J. Med.2009; 360:2605-15.
Li Z, Watanabe T, Hatta M, et al. Mutational analysis of conserved amino acids in the influenza A virus nucleoprotein. J. Virol.2009; 83:4153-62.
Newcomb LL, Kuo RL, Ye Q, et al. Interaction of the influenza a virus nucleocapsid protein with the viral RNA polymerase potentiates unprimed viral RNA replication. J. Virol.2009; 83:29-36.
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