|Immunogen||Influenza A, strain USSR (H1N1)|
|Shelf Life||18 months from the date of despatch.|
|Target/Specificity||Goat anti-Influenza A H1N1 polyclonal antibody is specific for Influenza A virus H1N1 by Haemagglutination inhibition.This goat anti-Influenza A H1N1 polyclonal antibody does not react with Influenza B, RSV, Para 1-3 or Adenovirus. It does not react with HEp-2 cells but may react with some chicken cellular proteins.Influenza type A viruses are divided into subtypes based on the antigenic differences of two viral surface proteins, hemagglutinin (H) and neuraminidase (N). On infection of the respiratory tract, the hemagglutinin molecule binds to sialic acid-containing receptors on the epithelial cells resulting in endocytosis. Once the virus has been engulfed, the hemagglutinin allows the viral membrane to fuse with the endosomal membrane. Neuraminidase functions to aid viral release from host cells by cleaving terminal sialic acid residues from carbohydrate moieties on the cell surface. Viral release also requires the interaction of the viral M1 protein with the celular scaffold G-like protein RACK1(Demirovet al.2012).Subtype antigenic variations result from a process known as antigenic drift whereby these surface proteins constantly mutate in order to evade the host immune repspone. Subtype A(H1N1) was the cause of Spanish flu pandemic that killed approximately 50,000,000 people between 1918-1919.|
|Preservative & Stabilisers||0.09% Sodium Azide (NaN3)|
|Storage||Store at +4℃ or at -20 ℃.|
|Precautions||Anti-Influenza A H1N1 Antibody (FITC) is for research use only and not for use in diagnostic or therapeutic procedures.|
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Provided below are standard protocols that you may find useful for product applications.
1. Demirov, D. et al. (2012) Interaction of influenza A virus matrix protein with RACK1 is required for virus release.Cell Microbiol. 14: 774-89. 2. Zielecki, F. et al. (2010) Virulence determinants of avian H5N1 influenza A virus in mammalian and avian hosts: The role of the C-terminal ESEV motif in the viral NS1 protein. J Virol. 117: 439 - 48 3. Kash, J.C. et al. (2011) Lethal Synergism of 2009 Pandemic H1N1 Influenza Virus and Streptococcus pneumoniae Coinfection Is Associated with Loss of Murine Lung Repair Responses.MBio. 2(5). pii: e00172-11. 4. Meunier, I. and von Messling, V. (2012) PB1-F2 Modulates Early Host Responses but Does not Affect the Pathogenesis of H1N1 Seasonal Influenza Virus. J Virol. 86: 4271-8. 5. Nicol, M.Q. et al. (2012) A novel family of peptides with potent activity against influenza A viruses.J Gen Virol. 93: 980-6. 6. Weinheimer, V.K. et al. (2012) Influenza A viruses target type II pneumocytes in the human lung.J Infect Dis. 206: 1685-94. 7. Weinheimer, V.K. et al. (2012) Influenza A viruses target type II pneumocytes in the human lung.J Infect Dis. 206 (11): 1685-94. 8. Kallfass, C. et al. (2013) Visualizing the beta interferon response in mice during infection with influenza A viruses expressing or lacking nonstructural protein 1.J Virol. 87 (12): 6925-30.
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