JavaScript is disabled in your browser. Please enable JavaScript to view this website.
AB252756

HRP Anti-Influenza A virus H1N1 antibody

Be the first to review this product! Submit a review

|

(1 Publication)

Goat Polyclonal Influenza A virus H1N1 antibody - conjugated to HRP. Suitable for ELISA, IHC-P and reacts with Influenza A samples. Cited in 1 publication. Immunogen corresponding to Virus preparation containing Influenza A virus H1N1 protein.

Key facts

Host species

Goat

Clonality

Polyclonal

Isotype

IgG

Conjugation

HRP

Excitation/Emission
Carrier free

No

Reacts with

Influenza A

Applications

IHC-P, ELISA

applications

Immunogen

The exact immunogen used to generate this antibody is proprietary information.

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "ELISA" : {"fullname" : "ELISA", "shortname":"ELISA"}, "IHCP" : {"fullname" : "Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections)", "shortname":"IHC-P"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Influenza A": { "ELISA-species-checked": "guaranteed", "ELISA-species-dilution-info": "", "ELISA-species-notes": "<p></p>", "IHCP-species-checked": "guaranteed", "IHCP-species-dilution-info": "", "IHCP-species-notes": "<p></p>" } } }

Properties and storage information

Form
Liquid
Purity
IgG fraction
Purification notes
IgG fraction covalently coupled to a highly purified preparation of horseradish peroxidase (RZ > 3). Care is taken to ensure adequate conjugation while preserving maximum enzyme activity. Free enzyme is absent. Estimated molar HRP:IgG substitution is 2–3.
Storage buffer
Preservative: 0.002% Thimerosal (merthiolate) Constituents: PBS, 0.1% BSA
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.

The Influenza A virus H1N1 is a subtype of the Influenza A virus that plays a role in viral replication and infection. This virus is known as 'swine flu' and has a protein structure with a mass of approximately 13.6 kDa. H1N1 virus is expressed on the surface of influenza virions and is responsible for the attachment of the virus to host cells. The hemagglutinin protein often referred to by its abbreviation 'HA' assists the virus to bind to the sialic acid receptors on epithelial cells in the respiratory tract facilitating viral entry into host cells.
Biological function summary

The H1N1 virus achieves this by functioning as an important antigenic protein important in immune response evasion. Hemagglutinin interacts with neuraminidase another major surface protein of the influenza virus forming a functional complex. This interaction is essential for viral infectivity as it mediates the fusion of the viral membrane with the host cell membrane allowing viral RNA to be released into the host cellular environment. The balance between hemagglutinin and neuraminidase functional activities regulates the virus's ability to infect and spread effectively.

Pathways

The H1N1 hemagglutinin is involved in the viral entry mechanism and has a role in the intracellular pathways of endocytosis and uncoating. The interaction with sialic acid receptors initiates the endocytosis pathway allowing the virus to enter the host cell while further processing involves the uncoating pathway which releases the viral RNA into the host cell interior. Neuraminidase aids in viral replication helping the virus to escape from the host cell and infect other cells. This interconnected activity of hemagglutinin and neuraminidase is essential for successful viral propagation.

The H1N1 strain relates closely to influenza epidemics and pandemics which lead to respiratory illnesses in humans. The virus's interaction with host immune response proteins such as interferon determines the severity of the disease. Hemagglutinin's variability can lead to antigenic drift posing challenges for vaccine development and increasing infection severity. The high mutation rate of H1N1 highlights its ongoing impact during influenza seasons and raises concerns over potential pandemic threats.

Product protocols

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

Publications (1)

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

Current protocols 4:e1030 PubMed38923763

2024

Applications of Surface Plasmon Resonance (SPR) to the Study of Diverse Protein-Ligand Interactions.

Applications

Unspecified application

Species

Unspecified reactive species

Dana M Burris,Samuel W Gillespie,Emma Joy Campbell,S Nick Ice,Vikas Yadav,William D Picking,Christian L Lorson,Kamal Singh
View all publications

Product promise

We are committed to supporting your work with high-quality reagents, and we're here for you every step of the way. In the unlikely event that one of our products does not perform as expected, you're protected by our Product Promise.
For full details, please see our Terms & Conditions

Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.

For licensing inquiries, please contact partnerships@abcam.com