Anti-Influenza NP [aNP-VHH1]

Description:

Recombinant monoclonal antibody to Influenza NP. Manufactured using AbAb’s Recombinant Platform with variable regions (i.e. specificity) from phage display aNP-VHH1.

Clone Name:

aNP-VHH1

Published Application(s):

crystallisation, IP, Neutralisation, WB, FC, IF

Published Species Reactivity:

Influenza

Product based on this clone:

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Ab01193-23.159 Anti-Influenza NP [aNP-VHH1]
Influenza
Rabbit IgG-Fc fusion
Purified
Ships in 4-5 weeks

UniProt Accession Number of Target Protein: P03466

Alternative Name(s) of Target: IAV NP; Influenza A virus nucleoprotein; Influenza A NP; Protein N; αNP-VHH1
Immunogen: Alpacas underwent 5 rounds of immunization with alcohol-fixed influenza virus PR8. The peripheral blood cells were collected and RNA from these cells was obtained. cDNA was generated, inserted into a M13 phagemid vector and transformed into bacteria. These were selected for by phage display-based panning. From the clones left, the aNP-VHH1 clone was selected.

Specificity: This antibody is specific for an epitope on the influenza virus A NP. The epitope is thought to overlap with a region of the protein responsible for several host protein interactions including importin-a and Mx proteins.

Application Notes: The binding specificity of this antibody has been confirmed with both a His tag (Hanke et al, 2016) and mCherry attached (Ashour et al, 2015). Its binding with IVA NP has been observed using X-ray crysallography (Ashour et al, 2015). It has been used for the immunoprecipitation of IVA NP and in western blotting. It has been shown to inhibit the nuclear localisation of its target ribonuclear protein, which disrupts the function of the virus (Ashour et al, 2015).

Antibody first published in: Ashour et al Intracellular Expression of Camelid Single-Domain Antibodies Specific for Influenza Virus Nucleoprotein Uncovers Distinct Features of Its Nuclear Localization J Virol. 2015 Mar 1; 89(5): 2792–2800 PMID:25540369
Note on publication: Discusses the generation of VHH fragments for influenza A by phage display, and how these disrupt the import of the ribonucleoprotein but not the nucleoprotein by its self.