| Catalog No. | Size | Price (USD) |
| 40199-V07H-10 | 10 µg | $188.10 |
| 40199-V07H-50 | 50 µg | $380.64 |
| 40199-V07H-100 | 100 µg | $765.73 |
General Information
| Formulation | Lyophilized from sterile PBS, pH 7.4. Please contact us for any concerns or special requirements. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA. |
| Endotoxin | < 1.0 EU per μg of the protein as determined by the LAL method |
| Shipping | In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature. Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise. |
| Stability & Storage | Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles. |
| Reconstitution | To find reconstitution info, click on 'COA' at the top of the page, enter the lot number and product size for the lot-specific COA. |
| Purity | > 90 % as determined by SDS-PAGE |
| Activity | Testing in progress |
| Protein Construction | A DNA sequence encoding the Influenza A virus (A/Aichi/2/1968(H3N2)) neuraminidase (Q75VQ4.1) (His36-Ile469) was expressed with a N-terminal polyhistidine tag. |
| Accession# | Q75VQ4.1 |
| Expressed Host | HEK293 Cells |
| Species | H3N2 |
| Predicted N Terminal | His |
| Molecule Mass | The recombinant neuraminidase of Influenza A virus (A/Aichi/2/1968 (H3N2)) comprises 453 amino acids and has a predicted molecular mass of 50.8 kDa. The apparent molecular mass of the protein is approximately 76.8 kDa in SDS-PAGE under reducing conditions. |
Image / Experimental Information
| Image 1 Alt Text | H3N2 Neuraminidase Protein 11178 |
| Image 1 URL | Source image |
Background Information
| Description | Neuraminidases are enzymes that cleave sialic acid groups from glycoproteins. Influenza neuraminidase is a type of neuraminidase found on the surface of influenza viruses that enables the virus to be released from the host cell. Influenza neuraminidase is composed of four identical subunits arranged in a square. It is normally attached to the virus surface through a long protein stalk. The active sites are in a deep depression on the upper surface. They bind to polysaccharide chains and clip off the sugars at the end. The surface of neuraminidase is decorated with several polysaccharide chains that are similar to the polysaccharide chains that decorate our cell surface proteins. Neuraminidase (NA) and hemagglutinin (HA) are major membrane glycoproteins found on the surface of the influenza virus. Hemagglutinin binds to the sialic acid-containing receptors on the surface of host cells during initial infection and at the end of an infectious cycle. Neuraminidase, on the other hand, cleaves the HA-sialic acid bondage from the newly formed virions and the host cell receptors during budding. Neuraminidase thus is described as a receptor-destroying enzyme that facilitates virus release and efficient spread of the progeny virus from cell to cell. Influenza antibody and influenza antibodies are very important research tools for influenza diagnosis, influenza vaccine development, and anti-influenza virus therapy development. The monoclonal or polyclonal antibody can be raised with protein based antigen or peptide-based antigen. Antibodies raised with protein-based antigen could have better specificity and/or binding affinity than antibodies raised with peptide based antigen, but the cost associated with the recombinant protein antigen is usually higher. Anti-influenza virus hemagglutinin (HA) monoclonal antibody or polyclonal antibody can be used for ELISA assay, western blotting detection, Immunohistochemistry (IHC), flow cytometry, neutralization assay, hemagglutinin inhibition assay, and early diagnosis of influenza viral infection. Sino Biological has developed state-of-the-art monoclonal antibody development technology platforms: mouse monoclonal antibody and rabbit monoclonal antibody. Our rabbit monoclonal antibody platform is one of a kind and offers some unique advantages over mouse monoclonal antibodies, such as high affinity, low cross-reactivity with rabbit polyclonal antibodies. |
| References |
|
title: Clonally expanded IgG, but not IgA, antibody-secreting cells preferentially target influenza nucleoprotein following homologous and heterologous infections.
authors: Andreas Agrafiotis; Raphael Kuhn; ...; Alexander Yermanos
journal: Journal of Immunology (Baltimore, Md. : 1950)
date: 2025-07-26
pmid: 40713886
doi: 10.1093/jimmun/vkaf144
cited_by_count: 0
techniques: Binding Assay; Cell Culture; Comparison; Concentration Assay; Enzyme-linked Immunosorbent Assay; Incubation; Plasmid Preparation; Transfection
bioz_score: 93
title: Clonally expanded IgG antibody-secreting cells preferentially target influenza nucleoprotein following homologous and heterologous infections
authors: Agrafiotis Andreas; Kuhn Raphael; ...; Yermanos Alexander
journal: bioRxiv
date: 2024-12-11
doi: 10.1101/2024.12.09.627526
cited_by_count: 0
techniques: Binding Assay; Cell Culture; Concentration Assay; Enzyme-linked Immunosorbent Assay; Incubation
bioz_score: 93
title: Tissue-specific sex differences in pediatric and adult immune cell composition and function
authors: Mahina Tabassum Mitul; Jenna M. Kastenschmidt; ...; Lisa E. Wagar
journal: Frontiers in Immunology
date: 2024-05-15
doi: 10.3389/fimmu.2024.1373537
pmcid: 11133680
cited_by_count: 0
bioz_score: 93
title: Hemagglutinin-specific antibodies and uses thereof
authors: Aziza Manceur; Anne Marcil; ...; Christine Gadoury
date: 2023-01-31
cited_by_count: 0
techniques: Incubation
bioz_score: 93
title: Longevity and Mechanism of Heterosubtypic Protection Induced by M2SR (M2-Deficient Single-Replication) Live Influenza Virus Vaccine in Mice
authors: Sally Sarawar; Claudia R. Gabaglia; ...; James Galloway
journal: Vaccines
date: 2022-12-13
pmid: 36560540
doi: 10.3390/vaccines10122131
pmcid: 9781428
cited_by_count: 4
techniques: Enzyme-linked Immunosorbent Assay; Infection; MANN-WHITNEY; Purification
bioz_score: 93
title: An AIE and ESIPT based neuraminidase fluorescent probe for influenza virus detection and imaging.
authors: Hao Chang; Yu Mei; ...; Luqing Shang
journal: Talanta
date: 2022-06-21
pmid: 35636364
doi: 10.1016/j.talanta.2022.123583
cited_by_count: 15
techniques: Fluorescence; Mutagenesis
bioz_score: 93
title: Quantification of Multivalent Interactions between Sialic Acid and Influenza A Virus Spike Proteins by Single-Molecule Force Spectroscopy.
authors: Jose Luis Cuellar-Camacho; Sumati Bhatia; ...; Rainer Haag
journal: Journal of the American Chemical Society
date: 2021-04-16
pmid: 32538085
doi: 10.1021/jacs.0c02852
cited_by_count: 20
techniques: Binding Assay; Incubation; Recombinant; Sample Prep
bioz_score: 93
title: Human antibody 3E1 targets the HA stem region of H1N1 and H5N6 influenza A viruses
authors: Wenshuai Wang; Xiaoyu Sun; ...; Bing Sun
journal: Nature Communications
date: 2016-12-02
pmid: 27910950
doi: 10.1038/ncomms13577
pmcid: 5477490
cited_by_count: 31
techniques: Affinity Chromatography; Amplification; Binding Assay; Purification; Recombinant; Transfection
bioz_score: 93
