Anti-Influenza A H3N2v, A/Minnesota/11/2010, Neuraminidase [B10] Antibody
![Anti-Influenza A H3N2v, A/Minnesota/11/2010, Neuraminidase [B10] Antibody](https://www.kerafast.com/MediaStorage/Product/Images/Large/1046_2001202001263210450.jpg "Anti-Influenza A H3N2v, A/Minnesota/11/2010, Neuraminidase [B10] Antibody")
This mouse monoclonal antibody (IgG2a) was raised against the NA of the swine-origin variant influenza A H3N2 virus A/Minnesota/11/2010.
Highlights:
- Reacts with the NA of the swine-origin H3N2 variant viruses that have infected humans and human seasonal H3N2 viruses circulated before the 2014-2015 influenza season, when an N-linked glycosylation site was introduced to residue 245 of NA (N2 subtype)
- Binds to an epitope consist of 14 amino acids within and around the active site
- Suitable for ELISA, immunofluorescence assay and NA inhibition assay
Influenza A H3N2 virus has long been circulating in humans together with H1N1 and influenza B viruses, resulting in annual influenza epidemics. While hemagglutinin (HA) on the surface of influenza virus is responsible for viral binding to and entry into host cells, neuraminidase (NA) as the second most abundant surface glycoprotein facilitates the release of the progeny virions for infecting more cells. NA is also the major target of FDA-approved antivirals that are used in treating influenza.
From the laboratory of Hongquan Wan, DVM, PhD, Food and Drug Administration.
This mouse monoclonal antibody (IgG2a) was raised against the NA of the swine-origin variant influenza A H3N2 virus A/Minnesota/11/2010.
Highlights:
- Reacts with the NA of the swine-origin H3N2 variant viruses that have infected humans and human seasonal H3N2 viruses circulated before the 2014-2015 influenza season, when an N-linked glycosylation site was introduced to residue 245 of NA (N2 subtype)
- Binds to an epitope consist of 14 amino acids within and around the active site
- Suitable for ELISA, immunofluorescence assay and NA inhibition assay
Influenza A H3N2 virus has long been circulating in humans together with H1N1 and influenza B viruses, resulting in annual influenza epidemics. While hemagglutinin (HA) on the surface of influenza virus is responsible for viral binding to and entry into host cells, neuraminidase (NA) as the second most abundant surface glycoprotein facilitates the release of the progeny virions for infecting more cells. NA is also the major target of FDA-approved antivirals that are used in treating influenza.
From the laboratory of Hongquan Wan, DVM, PhD, Food and Drug Administration.
| Product Type: | Antibody |
| Accession ID: | P0DOF9 |
| Isotype: | IgG2a |
| Clonality: | Monoclonal |
| Clone Name: | B10 |
| Reactivity: | Reacts with the NA of the swine-origin H3N2 variant viruses that have infected humans and human seasonal H3N2 viruses circulated before the 2014-2015 influenza season, when an N-linked glycosylation site was introduced to residue 245 of NA (N2 subtype) |
| Immunogen: | Purified MN/10 virus |
| Species Immunized: | Mouse |
| Epitope: | 14 amino acids overlapping with the NA (N2 subtype) active site |
| Purification Method: | Protein G |
| Buffer: | PBS, 0.05% (w/v) Sodium Azide |
| Tested Applications: | ELISA, ELLA, MUNANA |
| Storage: | -20C |
| Shipped: | Cold Packs |
- Hongquan W. Gao J. Yang H. Yang S. Harvey S. Chen Y. Zheng N. Chang J. Carney PJ. Li X. Plant E. Jiang Lianlian. Couzens L. Wang C. Strohmeier S, Wu WW. Shen RF. Krammer F. Cipollo JF. Wilso PC. Stevens J. Wan XF. Eichelberger MC. Ye Z. The neuraminidase of A(H3N2) influenza viruses circulating since 2016 is antigenically distinct from the A/Hong Kong/4801/2014 vaccine strain. Nat Microbiol. 2019 December. 4(12);2216-2225.
If you publish research with this product, please let us know so we can cite your paper.
