Abcam, ab308171, Anti-Influenza A virus H10N3 HA (Hemagglutinin) antibody [HL1559]

Size: 100µL
Rabbit Recombinant Monoclonal Hemagglutinin antibody. Carrier free. Suitable for IHC-P, ICC/IF and reacts with Transfected cell line - Influenza A samples.
Key facts
Host species:Rabbit,
Clonality:Monoclonal,
Clone number:HL1559,
Isotype:IgG,
Carrier free:Yes,
Reacts with:Influenza A,
Applications:ICC/IF, IHC-PSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.

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
Conjugation ready
Our carrier-free antibodies are typically supplied in a PBS-only formulation, purified and free of BSA, sodium azide and glycerol. This conjugation-ready format is designed for use with fluorochromes, metal isotopes, oligonucleotides, and enzymes, which makes them ideal for antibody labelling, functional and cell-based assays, flow-based assays (e.g. mass cytometry) and Multiplex Imaging applications.
Use our
conjugation kits
for antibody conjugates that are ready-to-use in as little as 20 minutes with 1 minute hands-on-time and 100% antibody recovery: available for fluorescent dyes, HRP, biotin and gold.

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Protein A, Storage buffer-pH: 7.4Constituents: PBS, 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-+4°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 Hemagglutinin often called hemagglutinin or the HA protein is a glycoprotein found on the surface of the Influenza A virus. It plays a mechanical role in the viral entry by binding to sialic acid residues on host cells. This binding allows the virus to attach and initiate infection. Hemagglutinin is known for its significant molecular mass of approximately 75 kDa. It expresses in various strains of the Influenza A virus including the Hong Kong strain and A/California/07/2009. It is an important component in determining the virus's ability to infect different host species.
Biological function summary
The HA protein functions in a critical step of the viral life cycle called fusion. During the infection process hemagglutinin undergoes a structural change that facilitates the fusion of the viral envelope with the host cell membrane. This fusion process is essential to release the viral genome into the host cell. Hemagglutinin generally operates as part of a trimeric complex which enhances its ability to interact with host cell receptors. This interaction is vital for the virus to efficiently invade the host cells and propagate the infection throughout the host.
Pathways
Hemagglutinin plays an important role in the viral fusion pathway and the innate immune response pathway. It interacts with proteins like neuraminidase another surface protein of the influenza virus which assists in the release of progeny viruses from infected cells. During the fusion pathway HA's structural changes allow the viral and cellular membranes to merge a step necessary for the virus to establish infection. Its involvement in the immune response pathway also prompts the host immune system to recognize and respond to viral threats.
Hemagglutinin is closely associated with influenza a contagious respiratory illness caused by influenza viruses. Mutations or antigenic shifts in HA contribute to seasonal flu epidemics and pandemics. The HA protein is a significant target for antibodies because its alteration can lead to vaccine inefficacy. Additionally it is associated with immune escape mechanisms where structural changes reduce antibody recognition. Researchers often study the interaction of hemagglutinin and antibodies like those targeting neuraminidase as these interactions are important for developing effective vaccines and antiviral therapies.