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AB91530

Anti-Swine Influenza A Hemagglutinin antibody

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(2 Publications)

Rabbit Polyclonal Hemagglutinin antibody. Suitable for ELISA, WB and reacts with Influenza A samples. Cited in 2 publications.

View Alternative Names

Hemagglutinin, HA

1 Images
Western blot - Anti-Swine Influenza A Hemagglutinin antibody (AB91530)
  • WB

Unknown

Western blot - Anti-Swine Influenza A Hemagglutinin antibody (AB91530)

All lanes:

Western blot - Anti-Swine Influenza A Hemagglutinin antibody (ab91530) at 2 µg/mL

Lane 1:

Seasonal Influenza A (H1N1) Hemagglutinin at 15 µg/mL

Lane 2:

Swine Influenza A (H1N1) Hemagglutinin at 15 µg/mL

Predicted band size: 63 kDa

false

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Influenza A

Applications

WB, ELISA

applications

Specificity

ab91530 is specific for the Swine Influenza A (H1N1) Hemagglutinin and will not recognize the corresponding Hemagglutinin from the seasonal H1N1 influenza virus.

Reactivity data

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Product details

The genetic make-up of this swine flu virus is unlike any other: it is an H1N1 strain that combines a triple assortment first identified in 1998 including human, swine, and avian influenza with two new pig H3N2 virus genes from Eurasia, themselves of recent human origin.

Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Purification notes
Affinity chromatography purified via peptide column.
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 (2)

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

Epigenetics & chromatin 17:11 PubMed38671530

2024

Reinforcement of repressive marks in the chicken primordial germ cell epigenetic signature: divergence from basal state resetting in mammals.

Applications

Unspecified application

Species

Unspecified reactive species

Clémence Kress,Luc Jouneau,Bertrand Pain

Biosensors & bioelectronics 58:33-9 PubMed24607620

2014

Metal enhanced fluorescence on nanoporous gold leaf-based assay platform for virus detection.

Applications

Unspecified application

Species

Unspecified reactive species

Syed Rahin Ahmed,Md Ashraf Hossain,Jung Youn Park,Soo-Hyung Kim,Dongyun Lee,Tetsuro Suzuki,Jaebeom Lee,Enoch Y Park
View all publications

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