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Influenza A H1N1 antibody

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Anti Influenza A H1N1 Antibody thumbnail image 1
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Published customer image:
Goat anti Influenza A H1N1 polyclonal antibody (5315-0064) used to label influenza virus infected tissues in ferrets (Mustela putorius furo) by immunohistochemistry on formalin fixed, paraffin embedded tissue sections.
Image caption:
AAV‐HA and AAV‐cHA have a protective effect in ferrets.
IHC staining of submucosal glands (SMG) (G) or bronchi (H) with an anti‐H1N1 polyclonal antibody (bar: 100 &mum; red: influenza antigen (Neufuchsin); blue: nuclei (hematoxylin)).

From: Demminger DE, Walz L, Dietert K, Hoffmann H, Planz O, Gruber AD, von Messling V, Wolff T.
Adeno-associated virus-vectored influenza vaccine elicits neutralizing and Fcγ receptor-activating antibodies.
EMBO Mol Med. 2020 May 8;12(5):e10938.
doi: 10.15252/emmm.201910938.
This image is from an open access article distributed under terms of a Creative Commons Attribution License.

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Goat anti Influenza A H1N1

Product Type
Polyclonal Antibody
Isotype
Polyclonal IgG
Specificity
Influenza A H1N1

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Product Code Applications Pack Size List Price Your Price Qty
5315-0064
Datasheet Datasheet Datasheet
SDS Safety Datasheet SDS
H IF P 1 ml loader
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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 cellular scaffold G-like protein RACK1 (Demirov et 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 response. Subtype A(H1N1) was the cause of Spanish flu pandemic that killed approximately 50,000,000 people between 1918-1919.

Target Species
Viral
Product Form
Purified IgG - liquid
Buffer Solution
Phosphate buffered saline
Preservative Stabilisers
<0.1% Sodium Azide (NaN3)
Immunogen
Influenza A, strain USSR (H1N1)
Approx. Protein Concentrations
IgG concentration 1.0 mg/ml
Regulatory
For research purposes only
Guarantee
12 months from date of despatch

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.

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.
Application Name Verified Min Dilution Max Dilution
Haemagglutination
Immunofluorescence
Immunohistology - Paraffin
Where this product has not been tested for use in a particular technique this does not necessarily exclude its use in such procedures. Suggested working dilutions are given as a guide only. It is recommended that the user titrates the product for use in their own system using the appropriate negative/positive controls.

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References for Influenza A H1N1 antibody

  1. 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
  2. Kash JC 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.
  3. Weinheimer, V.K. et al. (2012) Influenza A viruses target type II pneumocytes in the human lung.
    J Infect Dis. 206 (11): 1685-94.
  4. Nicol, M.Q. et al. (2012) A novel family of peptides with potent activity against influenza A viruses.
    J Gen Virol. 93: 980-6.
  5. 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.
  6. Demirov, D. et al. (2012) Interaction of influenza A virus matrix protein with RACK1 is required for virus release.
    Cell Microbiol. 14: 774-89.
  7. 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.
  8. Schliehe, C. et al. (2015) The methyltransferase Setdb2 mediates virus-induced susceptibility to bacterial superinfection.
    Nat Immunol. 16 (1): 67-74.
    9. View The Latest Product References
  9. Nicol, M.Q. et al. (2019) Lack of IFNγ signaling attenuates spread of influenza A virus in vivo and leads to reduced pathogenesis.
    Virology. 526: 155-164.
  10. Demminger, D.E. et al. (2020) Adeno-associated virus-vectored influenza vaccine elicits neutralizing and Fcγ receptor-activating antibodies.
    EMBO Mol Med. 12 (5): e10938.

Immunofluorescence

Immunohistology - Paraffin

RRID
AB_620739

5315-0064

154151

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