Influenza A Nucleoprotein antibody | AA5H
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 (clone GA2B).
- 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
0.09% Sodium Azide
- 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.
- Store at +4oC or at -20oC if preferred.
This product should be stored undiluted.
Storage in frost-free freezers is not recommended. Avoid repeated freezing and thawing as this may denature the antibody. Should this product contain a precipitate we recommend microcentrifugation before use.
- 18 months from date of despatch.
- For research purposes only
Applications of Influenza A Nucleoprotein antibody
|Application Name||Verified||Min Dilution||Max Dilution|
|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 © 2019 Bio-Rad Antibodies (formerly AbD Serotec)
Secondary Antibodies Available
Product Specific References
References for Influenza A Nucleoprotein antibody
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antiapoptotic signaling responses.
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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.
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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.
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Pauli, E.K. et al. (2008) Influenza A virus inhibits type I IFN signaling via NF-kappaB-dependent induction of SOCS-3 expression.
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Jamali, A. et al. (2010) A DNA vaccine-encoded nucleoprotein of influenza virus fails to induce cellular immune responses in a diabetic mouse model.
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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.
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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.
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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.
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Shu, Y. et al. (2010) Avian influenza A(H5N1) viruses can directly infect and replicate in human gut tissues.
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Hassan, I.H. et al. (2012) Influenza A viral replication is blocked by inhibition of the inositol-requiring enzyme 1 (IRE1) stress pathway.
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Brnic, D. et al. (2012) Borna disease virus infects human neural progenitor cells and impairs neurogenesis.
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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.
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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.
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Thompson, C.I. et al. (2006) Infection of human airway epithelium by human and avian strains of influenza a virus.
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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.
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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
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Sadewasser, A. et al. (2017) Quantitative proteomic approach identifies Vpr binding protein as novel host factor supporting influenza A virus infections in human cells.
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Kim HR et al. (2016) Ostrich ( Struthio camelus ) Infected with H5N8 Highly Pathogenic Avian Influenza Virus in South Korea in 2014.
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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.
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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.