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AB21304

Anti-Avian Influenza A Neuraminidase 抗体

Anti-Avian Influenza A Neuraminidase antibody

2

(1 Review)

|

(9 Publications)

Rabbit Polyclonal NRAM antibody. Suitable for WB, ELISA and reacts with Recombinant full length protein - Influenza A samples. Cited in 9 publications.

別名を表示する

Neuraminidase, NA

3 Images
ELISA - Anti-Avian Influenza A Neuraminidase antibody (AB21304)
  • ELISA

Supplier Data

ELISA - Anti-Avian Influenza A Neuraminidase antibody (AB21304)

Validation with Avian Influenza NA Protein Coating Antigen : Avian Influenza Neuraminidase recombinant protein, 2 μg/mL, incubated at 4˚C overnight. Detection Antibodies : ab21304, 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 (AB21304)
  • WB

Supplier Data

Western blot - Anti-Avian Influenza A Neuraminidase antibody (AB21304)

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

All lanes:

Western blot - Anti-Avian Influenza A Neuraminidase antibody (ab21304) 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

Western blot - Anti-Avian Influenza A Neuraminidase antibody (AB21304)
  • WB

PubMed

Western blot - Anti-Avian Influenza A Neuraminidase antibody (AB21304)

Expression of the H1 or N1 proteins by recombinant vaccinia viruses was detected by Western blotting. Vero cells in case of the VV-L constructs, or the avian cell line DF-1 [15] in case of MVA, were infected at a multiplicity of infection of 0.1 for 48 hours. MVA-H1-Ca or rVVL-H1-Ca infected cells were harvested by scraping or by adding trypsin. MVA-N1-Ca or rVVL-N1-Ca infected cells were harvested by scraping. Sonicated cell lysates were loaded onto 12% polyacrylamide gels and afterwards blotted on nitrocellulose membrane. To detect the H1 protein, a sheep antiserum against the A/California/7/2009 hemagglutinin (NIBSC 09/152) was used. Donkey-anti-sheep alkaline phosphatase-conjugated IgG was used as a secondary antibody. To detect the N1 protein ab21304 was utilized. Goat-anti-rabbit alkaline phosphatase-conjugated IgG was used as a secondary antibody. A whole virus vaccine H1N1 A/California/7/2009 [16] served as positive control.

Neuraminidase expression in chicken cells.

All lanes:

Western blot - Anti-Avian Influenza A Neuraminidase antibody (ab21304)

Predicted band size: 51 kDa

false

Image from Hessel A et al, PLoS One. 2010 Aug 16;5(8). pii: e12217, Fig 1.

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

ab21304 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.

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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 (9)

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

JCI insight 7: PubMed35852874

2022

The UIP/IPF fibroblastic focus is a collagen biosynthesis factory embedded in a distinct extracellular matrix.

Applications

Unspecified application

Species

Unspecified reactive species

Jeremy A Herrera,Lewis Dingle,M Angeles Montero,Rajamiyer V Venkateswaran,John F Blaikley,Craig Lawless,Martin A Schwartz

Viruses 14: PubMed35458460

2022

Characterization of Immune Response towards Generation of Universal Anti-HA-Stalk Antibodies after Immunization of Broiler Hens with Triple H5N1/NA-HA-M1 VLPs.

Applications

Unspecified application

Species

Unspecified reactive species

Beata Gromadzka,Milena Chraniuk,Lilit Hovhannisyan,Karolina Uranowska,Bogusław Szewczyk,Magdalena Narajczyk,Mirosława Panasiuk

Methods in molecular biology (Clifton, N.J.) 2183:331-356 PubMed32959252

2020

Attenuation Methods for Live Vaccines.

Applications

Unspecified application

Species

Unspecified reactive species

Dipasree Hajra,Akshay Datey,Dipshikha Chakravortty

mBio 11: PubMed32127444

2020

Heterosubtypic Protection Induced by a Live Attenuated Influenza Virus Vaccine Expressing Galactose-α-1,3-Galactose Epitopes in Infected Cells.

Applications

Unspecified application

Species

Unspecified reactive species

Li-Meng Yan,Sylvia P N Lau,Chek Meng Poh,Vera S F Chan,Michael C W Chan,Malik Peiris,Leo L M Poon

Journal of virology 89:10762-73 PubMed26269186

2015

Generation of Live Attenuated Influenza Virus by Using Codon Usage Bias.

Applications

WB

Species

Unspecified reactive species

Rebecca L Y Fan,Sophie A Valkenburg,Chloe K S Wong,Olive T W Li,John M Nicholls,Raul Rabadan,J S Malik Peiris,Leo L M Poon

Cell death & disease 4:e562 PubMed23538443

2013

Influenza A virus nucleoprotein induces apoptosis in human airway epithelial cells: implications of a novel interaction between nucleoprotein and host protein Clusterin.

Applications

WB

Species

Unspecified reactive species

S Tripathi,J Batra,W Cao,K Sharma,J R Patel,P Ranjan,A Kumar,J M Katz,N J Cox,R B Lal,S Sambhara,S K Lal

PloS one 5:e15556 PubMed21151571

2010

The low-pH stability discovered in neuraminidase of 1918 pandemic influenza A virus enhances virus replication.

Applications

Flow Cyt

Species

Influenza A

Tadanobu Takahashi,Yuuki Kurebayashi,Kumiko Ikeya,Takashi Mizuno,Keijo Fukushima,Hiroko Kawamoto,Yoshihiro Kawaoka,Yasuo Suzuki,Takashi Suzuki

PloS one 5:e12217 PubMed20808939

2010

A pandemic influenza H1N1 live vaccine based on modified vaccinia Ankara is highly immunogenic and protects mice in active and passive immunizations.

Applications

WB

Species

Unspecified reactive species

Annett Hessel,Michael Schwendinger,Daniela Fritz,Sogue Coulibaly,Georg W Holzer,Nicolas Sabarth,Otfried Kistner,Walter Wodal,Astrid Kerschbaum,Helga Savidis-Dacho,Brian A Crowe,Thomas R Kreil,P Noel Barrett,Falko G Falkner

Journal of immunology (Baltimore, Md. : 1950) 182:3063-71 PubMed19234203

2009

Vaccinia virus-based multivalent H5N1 avian influenza vaccines adjuvanted with IL-15 confer sterile cross-clade protection in mice.

Applications

WB

Species

Unspecified reactive species

Leo L M Poon,Y H Connie Leung,John M Nicholls,Pin-Yu Perera,Jack H Lichy,Masafumi Yamamoto,Thomas A Waldmann,J S Malik Peiris,Liyanage P Perera
View all publications

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