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AB91643

Anti-Swine H1N1 Neuraminidase antibody

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(1 Publication)

Rabbit Polyclonal NRAM antibody. Suitable for ELISA and reacts with Synthetic peptide - Influenza A virus (A/California/14/2009(H1N1)) samples. Cited in 1 publication.

View Alternative Names

Neuraminidase, NA

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ELISA - Anti-Swine H1N1 Neuraminidase antibody (AB91643)
  • ELISA

Unknown

ELISA - Anti-Swine H1N1 Neuraminidase antibody (AB91643)

ELISA using ab91643 at 1 μg/ml. Detects 2ng of Swine H1N1 Neuraminidase peptide.

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Influenza A virus (A/California/14/2009(H1N1))

Applications

ELISA

applications

Specificity

Specific for the novel S-OIV A H1N1 strain Neuraminidase and will not recognize the corresponding Neuraminidase sequence from the seasonal H1N1 influenza (A/Georgia/20/2006 (H1N1)).

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 H1N1 Neuraminidase also known as Sialidase is an enzyme that catalyzes the hydrolysis of terminal sialic acid residues from glycoproteins and glycolipids. It has a molecular mass of approximately 60 kDa. This enzyme appears on the surface of the Influenza A virus including swine flu strains. Neuraminidase plays a critical mechanical role in the viral life cycle by facilitating the release of progeny virus from infected host cells.
Biological function summary

In the context of the influenza virus Swine H1N1 Neuraminidase contributes to the spread of infection by breaking down mucins in the respiratory tract helping the virus to penetrate host cells. This protein functions as part of a complex with hemagglutinin another viral surface protein ensuring the continuity of virus attachment and release processes. This complementary interaction between neuraminidase and hemagglutinin supports efficient viral entry and exit maintaining the infection cycle.

Pathways

Swine H1N1 Neuraminidase is significant in two main biological pathways: viral entry and viral release from host cells. Neuraminidase breaks the link between viruses and the sialic acid residues present on host cell surfaces facilitating the budding of new viral particles. Hemagglutinin closely related through these pathways mediates initial binding and fusion with host membranes while neuraminidase functions to clear released viruses from decoy sites making them ready to infect new cells.

Neuraminidase from Swine H1N1 is an important factor in the pathogenesis of swine flu and related influenza pandemics. The activity of neuraminidase in coordination with hemagglutinin ensures the efficiency of viral infection and replication contributing to respiratory infections in humans and swine. Therapeutics targeting neuraminidase such as oseltamivir are important in controlling the spread and impact of these influenza types highlighting its role in antiviral treatment strategies.

Product protocols

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

Target data

Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Otherwise, infection would be limited to one round of replication. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. May facilitate viral invasion of the upper airways by cleaving the sialic acid moieties on the mucin of the airway epithelial cells. Likely to plays a role in the budding process through its association with lipid rafts during intracellular transport. May additionally display a raft-association independent effect on budding. Plays a role in the determination of host range restriction on replication and virulence. Sialidase activity in late endosome/lysosome traffic seems to enhance virus replication.
See full target information NA

Publications (1)

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Virology journal 20:183 PubMed37596622

2023

Influenza a virus regulates interferon signaling and its associated genes; MxA and STAT3 by cellular miR-141 to ensure viral replication.

Applications

Unspecified application

Species

Unspecified reactive species

Mai Alalem,Emad Dabous,Ahmed M Awad,Nedaa Alalem,Adel A Guirgis,Samir El-Masry,Hany Khalil
View all publications

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