Abcam, ab318988, Anti-influenza A H1N1 (A/California/07/2009) neuraminidase antibody [CD6]

Size: 20µg / 100µg / 1mg
Mouse Recombinant Monoclonal N1, influenza H1N1, A/California/07/2009 antibody. Suitable for ICC/IF, I-ELISA and reacts with Transfected cell line - Influenza A virus (A/California/07/2009(H1N1)), Recombinant full length protein - Influenza A virus (A/California/07/2009(H1N1)) samples.
Key facts
Host species:Mouse,
Clonality:Monoclonal,
Clone number:CD6,
Isotype:IgG2a,
Carrier free:No,
Reacts with:Influenza A virus (A/California/07/2009(H1N1)),
Applications:I-ELISA, ICC/IFSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Immunogen:The exact immunogen used to generate this antibody is proprietary information.,
Specificity:This antibody reacts with Influenza A virus H1N1, A/California/07/2009 neuraminidase and does not react with Influenza A virus H1N1, A/Brisbane/59/2007 neuraminidase or Influenza A virus H7N9, A/Anhui/1/2013 neuraminidase.

Product details:
What are the advantages of a recombinant monoclonal antibody?
This product is a recombinant monoclonal antibody, which offers several advantages including:
- High batch-to-batch consistency and reproducibility
- Improved sensitivity and specificity
- Long-term security of supply
- Animal-free batch production
For more information, read more on
recombinant antibodies
Want a custom formulation?
This antibody clone is manufactured by Abcam. If you require a custom buffer formulation or conjugation for your experiments, please contact orders@abcam.com

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Protein A, Storage buffer-pH: 7.2 - 7.4Preservative: 0.01% Sodium azideConstituents: PBS, 40% Glycerol (glycerin, glycerine), 0.05% BSA, Shipped at conditions-Blue Ice, Appropriate short-term storage duration-1-2 weeks, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--20°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Influenza A H1N1 (A/California/07/2009) neuraminidase also known as NA is an enzyme important for the viral life cycle. It cleaves sialic acid groups from glycoproteins facilitating the release of new virus particles from host cells. This process aids the spread of infection within the host. Neuraminidase of H1N1 has a molecular mass of around 60 kDa. It is expressed on the surface of the influenza virus where it functions to support the viral budding process.
Biological function summary
Neuraminidase enables the influenza virus to exit infected cells and invade new ones ensuring efficient viral dissemination. It functions as part of a complex with the viral hemagglutinin protein which helps the virus attach to the host cell surface before infection. Neuraminidase's enzymatic action counteracts hemagglutinin's binding by cutting sialic acid residues from host receptors an essential function for viral replication.
Pathways
Neuraminidase plays a role in the influenza viral budding and release pathway coordinating with hemagglutinin to manage the balance between virus attachment and release. This action relates to various antiviral research efforts aimed at blocking this process focusing on the hemagglutinin-neuraminidase balance. Interventions at this level may inhibit the virus' ability to proliferate highlighting the importance of neuraminidase in therapeutic pathways targeting influenza.
Neuraminidase is directly linked to influenza infection a respiratory illness with pandemic potential. Inhibitors like oseltamivir and zanamivir are designed to block neuraminidase activity preventing the virus' spread in the body. These inhibitors target the interaction between neuraminidase and sialic acid residues aiming to disrupt the pathogenesis of the influenza virus. This interaction offers a promising target for therapeutic strategies against influenza virus strains including potential drug-resistant variants.