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AB20711

Anti-Influenza B Virus Nucleoprotein antibody [B017]

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(15 Publications)

Anti-Influenza B Virus Nucleoprotein antibody [B017] (ab20711) is a mouse monoclonal antibody detecting Influenza B Virus Nucleoprotein in Western Blot, ICC/IF, ELISA. Suitable for Influenza B.

- Over 10 publications
- Trusted since 2005

View Alternative Names

Nucleoprotein, Nucleocapsid protein, Protein N, NP

1 Images
Immunocytochemistry/ Immunofluorescence - Anti-Influenza B Virus Nucleoprotein antibody [B017] (AB20711)
  • ICC/IF

PubMed

Immunocytochemistry/ Immunofluorescence - Anti-Influenza B Virus Nucleoprotein antibody [B017] (AB20711)

Immunofluorescence analysis of A549 cells 8 hours after infection with Influenza B, staining Influenza B Virus Nucleoprotein with ab20711.

Image from Dauber B et al., PLoS Pathog. 2009 Jun;5(6):e1000473. doi: 10.1371/journal.ppat.1000473. Epub 2009 Jun 12.; Fig 4.; June 12, 2009, PLoS Pathog 5(6): e1000473.

Key facts

Host species

Mouse

Clonality

Monoclonal

Clone number

B017

Isotype

IgG2b

Carrier free

No

Reacts with

Influenza B

Applications

WB, ICC/IF, ELISA

applications

Immunogen

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

Virus preparation containing Influenza B virus (strain B/Singapore/222/1979) protein.

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Reactivity data

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Product details

What is this antibody validated in?
Anti-Influenza B Virus Nucleoprotein antibody [B017] (ab20711) is a mouse monoclonal antibody and is validated for use in Western Blot (WB), Immunocytochemistry/immunofluorescence (ICC/IF), ELISA in Influenza B samples.

Trusted by the scientific community
Anti-Influenza B Virus Nucleoprotein [B017] (ab20711) was first used in a scientific publication in 2005 and has been cited over 10 times in peer-reviewed journals.
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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein G
Purification notes
>95% pure (SDS-PAGE). Protein G Affinity chromatography.
Storage buffer
pH: 7.5 Preservative: 0.09% Sodium azide Constituents: PBS
Shipped at conditions
Blue Ice
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
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Supplementary information

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

The Influenza B Virus Nucleoprotein often known as NP or flu B NP is an essential structural protein with a molecular weight of approximately 56 kDa. It plays a role in the influenza B virus lifecycle by encapsidating the viral RNA forming the ribonucleoprotein complex important for viral replication and transcription. This protein expresses in the host cell's cytoplasm and nucleus facilitating the export of vRNPs from the nucleus.
Biological function summary

The ribonucleoprotein complex formation involves nucleoproteins assembling with the viral RNA and polymerase subunits securing the genome for replication and transcription. NP interacts with both the polymerase basic 2 (PB2) and polymerase acidic (PA) proteins forming a vital part of the complex. This interaction allows the viral RNA to maintain its structure and function effectively during the virus infection cycle aiding both Influenza A and B viruses.

Pathways

NP participates in the viral replication pathway supporting the influenza virus propagation in infected cells. It associates closely with viral RNA polymerases and is integral to the transcription and replication of the viral RNA genome. Other key proteins involved in these pathways include the polymerase basic 1 (PB1) protein essential for synthesizing viral mRNA and the matrix protein (M1) which aids in vRNA encapsidation and budding.

NP relates closely to influenza B infections contributing to the clinical symptoms of flu B such as fever and respiratory issues. This protein is also a potential target for vaccine and therapeutic development against influenza B. NP shares a connection with the M2 protein another target in antiviral strategies given its role in proton channel activity and viral uncoating. Understanding NP's role can guide the creation of flu B antibodies and influenza A and B antibodies to reduce disease severity or prevent flu infections.
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Product protocols

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

Encapsidates the negative strand viral RNA, protecting it from nucleases. The encapsidated genomic RNA is termed the ribonucleoprotein (RNP) and serves as template for transcription and replication. The RNP needs to be localized in the host nucleus to start an infectious cycle, but is too large to diffuse through the nuclear pore complex. NP comprises at least 2 nuclear localization signals that are responsible for the active RNP import into the nucleus through cellular importin alpha/beta pathway. Later in the infection, nclear export of RNPs are mediated through viral proteins NEP interacting with M1 which binds nucleoproteins. It is possible that nucleoprotein binds directly host exportin-1/XPO1 and plays an active role in RNPs nuclear export. M1 interaction with RNP seems to hide nucleoprotein's nuclear localization signals. Soon after a virion infects a new cell, M1 dissociates from the RNP under acidification of the virion driven by M2 protein. Dissociation of M1 from RNP unmasks nucleoprotein's nuclear localization signals, targeting the RNP to the nucleus.
See full target information NP
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Publications (15)

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

Nature 618:590-597 PubMed37258672

2023

A pan-influenza antibody inhibiting neuraminidase via receptor mimicry.

Applications

Unspecified application

Species

Unspecified reactive species

Corey Momont,Ha V Dang,Fabrizia Zatta,Kevin Hauser,Caihong Wang,Julia di Iulio,Andrea Minola,Nadine Czudnochowski,Anna De Marco,Kaitlin Branch,David Donermeyer,Siddhant Vyas,Alex Chen,Elena Ferri,Barbara Guarino,Abigail E Powell,Roberto Spreafico,Samantha S Yim,Dale R Balce,Istvan Bartha,Marcel Meury,Tristan I Croll,David M Belnap,Michael A Schmid,William Timothy Schaiff,Jessica L Miller,Elisabetta Cameroni,Amalio Telenti,Herbert W Virgin,Laura E Rosen,Lisa A Purcell,Antonio Lanzavecchia,Gyorgy Snell,Davide Corti,Matteo Samuele Pizzuto

Frontiers in microbiology 13:1067725 PubMed36704555

2023

Antiviral effects of Atractyloside A on the influenza B virus (Victoria strain) infection.

Applications

Unspecified application

Species

Unspecified reactive species

Jicheng Han,Xiangyu Zhu,Zihan Gao,Yan Xiao,Jinxin Zhang,Peng Wang,Jinbo Fang,Yiquan Li,Yilong Zhu,Yue Li,Ningyi Jin,Huijun Lu,Dazhuan Lin,Wenshen Liu

iScience 24:102970 PubMed34471863

2021

Endoplasmic reticulum stress response and bile acid signatures associate with multi-strain seroresponsiveness during elderly influenza vaccination.

Applications

Unspecified application

Species

Unspecified reactive species

Christophe Carre,Glenn Wong,Vipin Narang,Crystal Tan,Joni Chong,Hui Xian Chin,Weili Xu,Yanxia Lu,Michelle Chua,Michael Poidinger,Paul Tambyah,Ma Nyunt,Tze Pin Ng,Daniel Larocque,Catherine Hessler,Nabil Bosco,Laurence Quemeneur,Anis Larbi

PLoS pathogens 17:e1009340 PubMed33596274

2021

Mitochondrial morphodynamics alteration induced by influenza virus infection as a new antiviral strategy.

Applications

Unspecified application

Species

Unspecified reactive species

Irene Pila-Castellanos,Diana Molino,Joe McKellar,Laetitia Lines,Juliane Da Graca,Marine Tauziet,Laurent Chanteloup,Ivan Mikaelian,Laurène Meyniel-Schicklin,Patrice Codogno,Jacky Vonderscher,Cédric Delevoye,Olivier Moncorgé,Eric Meldrum,Caroline Goujon,Etienne Morel,Benoit de Chassey

Journal of virology 93: PubMed31217244

2019

ANP32 Proteins Are Essential for Influenza Virus Replication in Human Cells.

Applications

Unspecified application

Species

Unspecified reactive species

Ecco Staller,Carol M Sheppard,Peter J Neasham,Bhakti Mistry,Thomas P Peacock,Daniel H Goldhill,Jason S Long,Wendy S Barclay

Proceedings of the National Academy of Sciences of 116:17399-17408 PubMed31391303

2019

An influenza virus-triggered SUMO switch orchestrates co-opted endogenous retroviruses to stimulate host antiviral immunity.

Applications

Unspecified application

Species

Unspecified reactive species

Nora Schmidt,Patricia Domingues,Filip Golebiowski,Corinna Patzina,Michael H Tatham,Ronald T Hay,Benjamin G Hale

Methods in molecular biology (Clifton, N.J.) 1602:205-238 PubMed28508223

2017

Reverse Genetics of Influenza B Viruses.

Applications

Unspecified application

Species

Unspecified reactive species

Aitor Nogales,Daniel R Perez,Jefferson Santos,Courtney Finch,Luis Martínez-Sobrido

Scientific reports 7:43893 PubMed28272419

2017

Acid phosphatase 2 (ACP2) is required for membrane fusion during influenza virus entry.

Applications

Unspecified application

Species

Unspecified reactive species

Jihye Lee,Jinhee Kim,Kidong Son,Anne-Laure Pham Humg d'Alexandry d'Orengiani,Ji-Young Min

Virus research 213:69-81 PubMed26590325

2015

Replication-competent fluorescent-expressing influenza B virus.

Applications

Unspecified application

Species

Unspecified reactive species

Aitor Nogales,Irene Rodríguez-Sánchez,Kristen Monte,Deborah J Lenschow,Daniel R Perez,Luis Martínez-Sobrido

Journal of virology 89:4818-26 PubMed25673727

2015

Domestic pigs are susceptible to infection with influenza B viruses.

Applications

Unspecified application

Species

Unspecified reactive species

Zhiguang Ran,Huigang Shen,Yuekun Lang,Elizabeth A Kolb,Nuri Turan,Laihua Zhu,Jingjiao Ma,Bhupinder Bawa,Qinfang Liu,Haixia Liu,Megan Quast,Gabriel Sexton,Florian Krammer,Ben M Hause,Jane Christopher-Hennings,Eric A Nelson,Juergen Richt,Feng Li,Wenjun Ma
View all publications
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