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AB191862

Anti-Avian Influenza A Neuraminidase antibody - N-terminal

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(1 Publication)

Rabbit Polyclonal NRAM antibody. N-terminal. Suitable for ELISA, WB and reacts with Influenza A, Recombinant full length protein - Influenza A samples. Cited in 1 publication.

View Alternative Names

Neuraminidase, NA

3 Images
ELISA - Anti-Avian Influenza A Neuraminidase antibody - N-terminal (AB191862)
  • ELISA

Supplier Data

ELISA - Anti-Avian Influenza A Neuraminidase antibody - N-terminal (AB191862)

Validation with H7N9 NA Protein Coating Antigen : H7N9 Neuraminidase recombinant protein, 2 μg/mL, incubated at 4˚C overnight. Detection Antibodies : ab191862, dilution : 1-1000 ng/mL, incubated at RT for 1 hr. Secondary Antibodies : Goat anti-rabbit HRP at 1/10000, incubated at RT for 1 hr.

ELISA - Anti-Avian Influenza A Neuraminidase antibody - N-terminal (AB191862)
  • ELISA

Supplier Data

ELISA - Anti-Avian Influenza A Neuraminidase antibody - N-terminal (AB191862)

ab191862 at 1 μg/ml detects 10 ng of H7N9 [Influenza A virus (A/Shanghai/02/2013(H7N9))] Neuraminidase peptide, and not 10 ng of H7N9 [Influenza A virus (A/blue-winged teal/Ohio/566/2006(H7N9))] Neuraminidase peptide in ELISA.

Western blot - Anti-Avian Influenza A Neuraminidase antibody - N-terminal (AB191862)
  • WB

Supplier Data

Western blot - Anti-Avian Influenza A Neuraminidase antibody - N-terminal (AB191862)

1h incubation at RT in 5% NFDM/TBST.

All lanes:

Western blot - Anti-Avian Influenza A Neuraminidase antibody - N-terminal (ab191862) at 1 µg/mL

Lane 1:

H7N9 Neuraminidase recombinant protein at 50 ng

Lane 2:

H7N9 Neuraminidase recombinant protein at 100 ng

Secondary

All lanes:

Goat anti-rabbit IgG HRP conjugate at 1/10000 dilution

false

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Influenza A

Applications

WB, ELISA

applications

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 duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

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

Avian Influenza A Neuraminidase sometimes called N1 or neuraminidase protein is a viral enzyme with significant mechanical functions in the life cycle of influenza viruses. This enzyme a glycoprotein with an approximate mass of 470 kDa is expressed on the surface of the influenza virus particles. Neuraminidase cleaves sialic acid residues from glycoproteins and glycolipids facilitating the release of newly formed viral particles from infected host cells. This action helps the virus to spread efficiently and infect more cells.
Biological function summary

In the influenza virus life cycle the neuraminidase protein helps in preventing viral self-aggregation and assists in viral movement within the host. It is not part of a complex but functions in coordination with the hemagglutinin protein. Both neuraminidase and hemagglutinin are found on the viral envelope and play important roles in the viral infection process with hemagglutinin binding to host cell receptors and neuraminidase aiding in viral egress.

Pathways

Neuraminidase activity is integral to the sialic acid metabolic pathway ensuring the process of viral particle release is efficient. Neuraminidase works alongside hemagglutinin in the infection cycle with the two proteins together maintaining equilibrium necessary for efficient viral replication and dissemination. Additionally neuraminidase is involved in the neuraminidase inhibitor pathway which is targeted for antiviral drug development that block its function to prevent virus spread.

Avian influenza neuraminidase is most associated with influenza infections specifically avian influenza affecting both birds and occasionally humans. Antigenic variation in neuraminidase leads to the emergence of new strains complicating vaccine development and treatment strategies. Neuraminidase also plays a role in swine flu pathogenesis interacting with host proteins and hemagglutinin to mediate infection. Efforts to create avian antibodies target neuraminidase aiming to develop therapies that can either prevent or limit the spread of these infections.

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)

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

Journal of inflammation research 18:8153-8171 PubMed40557057

2025

Probiotic Bifico Ameliorates Depression- and Anxiety-Like Behaviors Induced by Estrogen Deficiency via NLRP3 Inflammasome Inhibition.

Applications

Unspecified application

Species

Unspecified reactive species

Xia Yu,Xiurong Yu,Yang Yang,Wei Cheng,Mingxiu Shi,Li Chen,Xiongle Zhang,Yongjun Xu
View all publications

Product promise

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