Mouse anti Influenza A Nucleoprotein antibody, clone AA5H
recognizes an epitope within Influenza virus A nucleoprotein. Mouse anti Influenza A Nucleoprotein antibody, clone AA5H can be used in influenza A IFA typing in conjunction with MCA401
- Target Species
- Product Form
- Purified IgG - liquid
- Purified IgG prepared by affinity chromatography on Protein A from tissue culture supernatant.
- Buffer Solution
- Phosphate buffered saline
- Preservative Stabilisers
- Influenza A / Puerto Rico / 8 / 34 (H1N1) and A/Bangkok / 1 / 79 (H3N2) viruses.
- Approx. Protein Concentrations
- IgG concentration 1.0 mg/ml
- Fusion Partners
- Spleen cells from BALB/c mice were fused with cells of the P3 Ag8.653 mouse myeloma cell line.
- This product is shipped at ambient temperature. It is recommended to aliquot and store at -20°C on receipt. When thawed, aliquot the sample as needed. Keep aliquots at 2-8°C for short term use (up to 4 weeks) and store the remaining aliquots at -20°C.
Avoid repeated freezing and thawing as this may denature the antibody. Storage in frost-free freezers is not recommended.
- 12 months from date of despatch
- For research purposes only
This product has been reported to work in the following applications. This information is derived from testing within our laboratories, peer-reviewed publications or personal communications from the originators. Please refer to references indicated for further information. For general protocol recommendations, please visit the antibody protocols page.
Applications of Influenza A Nucleoprotein antibody
|Immunohistology - Paraffin
Where this antibody has not been tested for use in a particular technique this does not necessarily exclude its use in such procedures. It is recommended that the user titrates the antibody for use in their own system using appropriate negative/positive controls.
Copyright © 2021 Bio-Rad Antibodies (formerly AbD Serotec)
Secondary Antibodies Available
Application Based External Images
Immunohistology - Paraffin
Product Specific References
References for Influenza A Nucleoprotein antibody
Herold, S. et al. (2006) Alveolar epithelial cells direct monocyte transepithelial migration upon influenza virus infection: impact of chemokines and adhesion molecules.
J Immunol. 177 (3): 1817-24.
Ehrhardt, C. et al. (2007) Influenza A virus NS1 protein activates the PI3K/Akt pathway to mediate
antiapoptotic signaling responses.
J Virol. 81: 3058-67.
Ehrhardt, C. et al. (2007) Activation of phosphatidylinositol 3-kinase signaling by the nonstructural NS1 protein is not conserved among type A and B influenza viruses.
J Virol. 81: 12097-100.
Matarrese, P. et al. (2011) Pepstatin A alters host cell autophagic machinery and leads to a decrease in influenza A virus production.
J Cell Physiol. 226 (12): 3368-77.
Nencioni, L. et al. (2009) Bcl-2 expression and p38MAPK activity in cells infected with influenza A virus: impact on virally induced apoptosis and viral replication.
J Biol Chem. 284: 16004-15.
Pauli, E.K. et al. (2008) Influenza A virus inhibits type I IFN signaling via NF-kappaB-dependent induction of SOCS-3 expression.
PLoS Pathog. 4(11): e1000196.
Jamali, A. et al. (2010) A DNA vaccine-encoded nucleoprotein of influenza virus fails to induce cellular immune responses in a diabetic mouse model.
Clin Vaccine Immunol. 17: 683-7.
Ehrhardt, C. et al. (2007) A polyphenol rich plant extract, CYSTUS052, exerts anti influenza virus activity in cell culture without toxic side effects or the tendency to induce viral resistance.
Antiviral Res. 76: 38-47.
Seitz, C. et al. (2010) High yields of influenza A virus in Madin-Darby canine kidney cells are promoted by an insufficient interferon-induced antiviral state.
J Gen Virol. 91: 1754-63.
Gabay, C. et al. (2011) Impact of synthetic and biologic disease-modifying antirheumatic drugs on antibody responses to the AS03-adjuvanted pandemic influenza vaccine: a prospective, open-label, parallel-cohort, single-center study.
Arthritis Rheum. 63 (6): 1486-96.
Luig, C. et al. (2010) MAP kinase-activated protein kinases 2 and 3 are required for influenza A virus propagation and act via inhibition of PKR.
FASEB J. 24: 4068-77.
Shu, Y. et al. (2010) Avian influenza A(H5N1) viruses can directly infect and replicate in human gut tissues.
J Infect Dis. 201: 1173-7.
Hassan, I.H. et al. (2012) Influenza A viral replication is blocked by inhibition of the inositol-requiring enzyme 1 (IRE1) stress pathway.
J Biol Chem. 287 (7): 4679-89.
Brnic, D. et al. (2012) Borna disease virus infects human neural progenitor cells and impairs neurogenesis.
J Virol. 86 (5): 2512-22.
Hrincius, E.R. et al. (2011) Phosphatidylinositol-3-kinase (PI3K) is activated by influenza virus vRNA via the pathogen pattern receptor Rig-I to promote efficient type I interferon production.
Cell Microbiol. 13: 1907-19.
Koerner, I. et al. (2012) Altered receptor specificity and fusion activity of the haemagglutinin contribute to high virulence of a mouse-adapted influenza A virus.
J Gen Virol. 93 (Pt 5): 970-9.
Thompson, C.I. et al. (2006) Infection of human airway epithelium by human and avian strains of influenza a virus.
J Virol. 80: 8060-8.
Gao, R. et al. (2010) A systematic molecular pathology study of a laboratory confirmed H5N1 human case.
PLoS One. 5: e13315.
Matthaei M et al. (2013) Highly pathogenic H5N1 influenza A virus strains provoke heterogeneous IFN-α/β responses that distinctively affect viral propagation in human cells.
PLoS One. 8 (2): e56659.
Wörmann, X. et al. (2016) Genetic characterization of an adapted pandemic 2009 H1N1 influenza virus that reveals improved replication rates in human lung epithelial cells
Virology. 492: 118-29.
Sadewasser, A. et al. (2017) Quantitative proteomic approach identifies Vpr binding protein as novel host factor supporting influenza A virus infections in human cells.
Mol Cell Proteomics. pii: mcp.M116.065904. [Epub ahead of print]
Kim HR et al. (2016) Ostrich ( Struthio camelus ) Infected with H5N8 Highly Pathogenic Avian Influenza Virus in South Korea in 2014.
Avian Dis. 60 (2): 535-9.
Dick, A. et al. (2015) Role of nucleotide binding and GTPase domain dimerization in dynamin-like myxovirus resistance protein A for GTPase activation and antiviral activity.
J Biol Chem. 290 (20): 12779-92.
Shoji, M. et al. (2015) Bakuchiol Is a Phenolic Isoprenoid with Novel Enantiomer-selective Anti-influenza A Virus Activity Involving Nrf2 Activation.
J Biol Chem. 290 (46): 28001-17.
Thulasi Raman, S.N. et al. (2016) DDX3 Interacts with Influenza A Virus NS1 and NP Proteins and Exerts Antiviral Function through Regulation of Stress Granule Formation.
J Virol. 90 (7): 3661-75.
Youchan, B. et al. (2018) Pathological lesions and antigen localization in chicken, ducks and Japanese quail naturally infected by novel highly pathogenic avian influenza (H5N6), Korea, 2016
J Prev Vet Med. 42 (3): 91-8.
Sid, H. et al. (2017) Interaction of Influenza A Viruses with Oviduct Explants of Different Avian Species.
Front Microbiol. 8: 1338.
Prokopyeva, E.A. et al. (2019) Pathology of A(H5N8) (Clade 184.108.40.206) Virus in Experimentally Infected Chickens and Mice.
Interdiscip Perspect Infect Dis. 2019: 4124865.
Calmy, A. et al. (2012) Strong serological responses and HIV RNA increase following AS03-adjuvanted pandemic immunization in HIV-infected patients.
HIV Med. 13 (4): 207-18.
Mayr, J. et al. (2018) Unravelling the Role of O-glycans in Influenza A Virus Infection.
Sci Rep. 8 (1): 16382.
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