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AB91641

Anti-Swine Influenza A Hemagglutinin antibody

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(3 Publications)

Rabbit Polyclonal Hemagglutinin antibody. Suitable for ELISA, WB and reacts with Influenza A samples. Cited in 3 publications.

View Alternative Names

Hemagglutinin, HA

1 Images
Western blot - Anti-Swine Influenza A Hemagglutinin antibody (AB91641)
  • WB

Unknown

Western blot - Anti-Swine Influenza A Hemagglutinin antibody (AB91641)

All lanes:

Western blot - Anti-Swine Influenza A Hemagglutinin antibody (ab91641) at 2 µg/mL

Lane 1:

Recombinant seasonal influenza Hemagglutinin

Lane 2:

Recombinant Swine Influenza A (H1N1) Hemagglutinin

Predicted band size: 61 kDa

false

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Influenza A

Applications

ELISA, WB

applications

Specificity

Specific for the Swine Influenza A (H1N1) Hemagglutinin. Does not bind the corresponding Hemagglutinin from seasonal H1N1 influenza virus.

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7.2 Preservative: 0.02% Sodium azide Constituents: PBS
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
+4°C

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Swine Influenza A Hemagglutinin often called HA is a surface glycoprotein on the influenza virus particularly H1N1 subtype. HA plays a central role in the initial attachment of the virus to the host cell by binding to sialic acid receptors. This binding facilitates the entry of the virus into the cell. Hemagglutinin weighs approximately 75 kDa. It is expressed on the envelope of the influenza virus and serves as an important antigenic target for immune response.
Biological function summary

Swine Influenza A Hemagglutinin functions to mediate the fusion between the viral envelope and the host cell membrane enabling the release of viral RNA into the host cell. HA operates as part of the viral protein complex within the influenza virus and is essential for viral infectivity. Its ability to mutate and change antigenic properties makes it a constant subject of study in immunology and vaccine development.

Pathways

Hemagglutinin directly interacts with the process of viral endocytosis and membrane fusion. It is a component of the viral life cycle pathway which includes the replication and assembly of viral particles. It works in concert with other viral proteins like neuraminidase which helps in the release of newly formed viral particles from the host cell. These pathways are critical for understanding how the influenza virus replicates and spreads in the host organism.

HA is primarily associated with Influenza illness outbreaks such as the H1N1 flu. This protein's ability to undergo frequent antigenic shifts and drifts complicates the development of effective vaccines making it a significant focus in flu research. Hemagglutinin's relationship with other proteins like neuraminidase contributes to the pathogenicity of flu viruses. Additionally it plays a role in cross-species transmission with strains such as G4 EA H1N1 raising concerns about potential pandemic sources.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore.. Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization either through clathrin-dependent endocytosis or through clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore.
See full target information HA

Publications (3)

Recent publications for all applications. Explore the full list and refine your search

mBio 11: PubMed32636247

2020

Staphylococcus aureus Lipase 1 Enhances Influenza A Virus Replication.

Applications

Unspecified application

Species

Unspecified reactive species

Mariya I Goncheva,Carina Conceicao,Stephen W Tuffs,Hui-Min Lee,Marlynne Quigg-Nicol,Ian Bennet,Fiona Sargison,Amy C Pickering,Saira Hussain,Andrew C Gill,Bernadette M Dutia,Paul Digard,J Ross Fitzgerald

The Journal of general virology 100:1079-1092 PubMed31169484

2019

Segment 2 from influenza A(H1N1) 2009 pandemic viruses confers temperature-sensitive haemagglutinin yield on candidate vaccine virus growth in eggs that can be epistatically complemented by PB2 701D.

Applications

Unspecified application

Species

Unspecified reactive species

Saira Hussain,Matthew L Turnbull,Rute M Pinto,John W McCauley,Othmar G Engelhardt,Paul Digard

Journal of virology 93: PubMed30381488

2019

Mutation of Influenza A Virus PA-X Decreases Pathogenicity in Chicken Embryos and Can Increase the Yield of Reassortant Candidate Vaccine Viruses.

Applications

Unspecified application

Species

Unspecified reactive species

Saira Hussain,Matthew L Turnbull,Helen M Wise,Brett W Jagger,Philippa M Beard,Kristina Kovacikova,Jeffery K Taubenberger,Lonneke Vervelde,Othmar G Engelhardt,Paul Digard
View all publications

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