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AB21305

Anti-Avian Influenza A Neuraminidase 抗体

Anti-Avian Influenza A Neuraminidase antibody

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(3 Publications)

Rabbit Polyclonal NRAM antibody. Suitable for ELISA, WB and reacts with Recombinant full length protein - Influenza A samples. Cited in 3 publications.

別名を表示する

Neuraminidase, NA

2 Images
ELISA - Anti-Avian Influenza A Neuraminidase antibody (AB21305)
  • ELISA

Supplier Data

ELISA - Anti-Avian Influenza A Neuraminidase antibody (AB21305)

Validation with Avian Influenza NA Protein Coating Antigen : Avian Influenza Neuraminidase recombinant protein, 2 μg/mL, incubated at 4˚C overnight. Detection Antibodies : ab21305, dilution : 1-1000 ng/mL, incubated at RT for 1 hr. Secondary Antibodies : Goat anti-rabbit HRP at 1/10000 dilution, incubated at RT for 1 hr.

Western blot - Anti-Avian Influenza A Neuraminidase antibody (AB21305)
  • WB

Supplier Data

Western blot - Anti-Avian Influenza A Neuraminidase antibody (AB21305)

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

All lanes:

Western blot - Anti-Avian Influenza A Neuraminidase antibody (ab21305) at 1 µg/mL

Lane 1:

Avian Influenza Neuraminidase recombinant protein at 50 ng

Lane 2:

Avian Influenza Neuraminidase recombinant protein at 100 ng

Secondary

All lanes:

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

Predicted band size: 51 kDa

false

Key facts

宿主種

Rabbit

クローン性

Polyclonal

アイソタイプ

IgG

キャリアフリー

No

交差種

Influenza A

アプリケーション

WB, ELISA

applications

特異性

ab21305 can be used for the detection of the Neuraminidase protein from the H5N1 strain of avian influenza A in ELISA and WB. It will detect 10 ng of free peptide at 1 μg/mL.

Reactivity data

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出荷温度及び保存条件

製品の状態
Liquid
精製方法
Affinity purification Immunogen
バッファー組成
pH: 7.2 Preservative: 0.02% Sodium azide Constituents: PBS
出荷温度
Blue Ice
短期保存温度
+4°C
長期保存温度
+4°C

補足情報

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.

製品プロトコール

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ターゲットの情報

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

文献 (3)

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

PloS one 7:e42363 PubMed22879951

2012

A VLP vaccine induces broad-spectrum cross-protective antibody immunity against H5N1 and H1N1 subtypes of influenza A virus.

Applications

Unspecified application

Species

Unspecified reactive species

Chia-Ying Wu,Yi-Chun Yeh,Jia-Tsrong Chan,Yu-Chih Yang,Ji-Rong Yang,Ming-Tsan Liu,Ho-Sheng Wu,Pei-Wen Hsiao

PloS one 5:e9784 PubMed20339535

2010

Mammalian expression of virus-like particles for advanced mimicry of authentic influenza virus.

Applications

ICC/IF, WB

Species

Unspecified reactive species, Unspecified reactive species

Chia-Ying Wu,Yi-Chun Yeh,Yu-Chih Yang,Ching Chou,Ming-Tsan Liu,Ho-Sheng Wu,Jia-Tsrong Chan,Pei-Wen Hsiao

Antiviral research 79:199-205 PubMed18453004

2008

In vitro evaluation of neuraminidase inhibitors using the neuraminidase-dependent release assay of hemagglutinin-pseudotyped viruses.

Applications

Unspecified application

Species

Unspecified reactive species

Ching-Yao Su,Shi-Yun Wang,Jiun-Jie Shie,King-Song Jeng,Nigel J Temperton,Jim-Min Fang,Chi-Huey Wong,Yih-Shyun E Cheng
View all publications

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