For immunochemical detection of influenza B HA
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Influenza B HA Rabbit Monoclonal Antibody (Clone 004)

Item No. 38077

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Synonyms
  • Influenza B Hemagglutinin
Immunogen
Recombinant influenza B virus HA
Clone Designation
004
Formulation (Request formulation change)
50 or 100 µl of protein A-affinity purified monoclonal antibody
Storage Buffer
0.2 μm filtered solution in PBS
Host
Rabbit
Isotype
IgG
Applications
ELISA, WB
Cross Reactivity
(+) H3N2 (A/Hong Kong/2671/2019 HA(+) Influenza B (B/Austria/1359417/2021)(Victoria lineage) HA Protein(+) Influenza B (B/Brisbane/60/2008) HA(+) Influenza B (B/Colorado/06/2017) HA(+) Influenza B (B/PHUKET/3073/2013) HA(+) Influenza B (B/Washington/02/2019) HA(-) H1N1 (A/Brisbane/02/2018) HA(-) H1N1 (A/California/04/2009) HA(-) H1N1 (A/Guangdong-Maonan/SWL1536/2019) / (A/Hawaii/70/2019) HA(-) H1N1 (A/Michigan/45/2015) HA(-) H1N1 (A/Puerto Rico/8/1934) HA(-) H1N1 (A/Wisconsin/588/2019) / (A/Victoria/2570/2019) HA(-) H3N2 (A/Brisbane/10/2007) HA(-) H3N2 (A/Cambodia/e0826360/2020) HA(-) H3N2 (A/Darwin/9/2021) HA Protein(-) H3N2 (A/Darwin/6/2021) HA Protein(-) H3N2 (A/Hong Kong/45/2019) HA(-) H3N2 (A/Hong Kong/4801/2014) HA(-) H3N2 (A/Kansas/14/2017) HA(-) H3N2 (A/Singapore/INFIMH-16-0019/2016) HA(-) H3N2 (A/Switzerland/9715293/2013) HA
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    20 µl

    $89

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    100 µl

    $378

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    Cayman Chemical
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    Product Description

    Influenza B HA is a type I membrane glycoprotein involved in receptor binding and virus-host cell fusion.1,2 It is produced as a precursor protein, HA0, which is composed of a stalk and head domain and forms homotrimers on the viral surface.3,4 The HA0 precursor is cleaved into subunits, HA1 and HA2, which are responsible for host cell surface receptor binding and endosomal membrane fusion, respectively, and this cleavage is required for endosomal fusion.4 For influenza B and influenza A, which are low pathogenic influenza viruses, cleavage occurs via trypsin-like proteases, such as transmembrane serine protease 2 (TMPRSS2), which is essential for influenza A HA, but not influenza B HA, cleavage.2,5,6 Cleaved influenza B HA binds to terminal α2,6-linked sialic acids on glycoproteins or glycolipids on the host cell surface via the receptor-binding domain in the HA1 subunit, which triggers endocytosis of the virus and trafficking of the vesicle into the endosome.3,7,8 The low pH environment of the endosome triggers viral rearrangement into a prefusion conformation, and the HA2 subunit facilitates fusion with the endosomal membrane to release viral ribonucleoproteins into the cytosol where they are relocated to the nucleus for viral replication.3 Cayman’s Influenza B HA Rabbit Monoclonal Antibody (Clone 004) can be used for ELISA and Western blot (WB) applications.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Gamblin, S.J., and Skehel, J.J. Influenza hemagglutinin and neuraminidase membrane glycoproteins. The Journal of Biological Chemisty 285(37), 28403-28409 (2010).

    2. Sakai, K., Ami, Y., Nakajima, N., et al. TMPRSS2 independency for haemagglutinin cleavage in vivo differentiates influenza B virus from influenza A virus. Sci. Rep. 6, 29430 (2016).

    3. Dou, D., Revol, R., Östbye, H., et al. Influenza A virus cell entry, replication, virion assembly and movement. Front. Immunol. 9, 1581 (2018).

    4. Russell, C.J. Hemagglutinin stability and its impact on influenza A virus infectivity, pathogenicity, and transmissibility in avians, mice, swine, seals, ferrets, and humans. Viruses 13(5), 746 (2021).

    5. Limburg, H., Harbig, A., Bestle, D., et al. TMPRSS2 is the major activating protease of influenza A virus in primary human airway cells and influenza B virus in human type II pneumocytes. J. Virol. 93(21), e00649-00619 (2019).

    6. Böttcher-Friebertshäuser, E., Lu, Y., Meyer, D., et al. Hemagglutinin activating host cell proteases provide promising drug targets for the treatment of influenza A and B virus infections. Vaccine 30(51), 7374-7380 (2012).

    7. Long, J.S., Mistry, B., Haslam, S.M., et al. Host and viral determinants of influenza A virus species specificity. Nat. Rev. Microbiol. 17(2), 67-81 (2019).

    8. Wang, Q., Tian, X., Chen, X., et al. Structural basis for receptor specificity of influenza B virus hemagglutinin. Proc. Natl. Acad. Sci. USA 104(43), 16874-16879 (2007).