Influenza A H3N2 Neuraminidase / NA (Active) sinobiological 40017-VNAHC
$400.00
In stock
SKU
40017-VNAHC
| Catalog No. | Size | Price (USD) |
| 40017-VNAHC-800 | 800 U | $414.71 |
General Information
| Formulation | Lyophilized from sterile PBS, 0.6% Triton X-100, 7% Trehalose, 6% Mannitol, 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 | Please contact us for more information. |
| 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. |
| Activity | Measured by its ability to cleave a fluorogenic substrate, 2’-(4-Methylumbelliferyl)-α-D-N-acetylneuraminic acid. One unit is defined as the amount of enzyme required to cleave 1 nmole of 2'-(4-Methylumbelliferyl)-α-D-N-acetylneuraminic acid per minute at pH 7.5 at 37℃. |
| Protein Construction | A DNA sequence encoding the Influenza A virus (A/Babol/36/2005 (H3N2)) neuraminidase (ACN50232.1) (His 36-Pro 459) was expressed, Collected cell lysates are validated for neuraminidase activity. |
| Accession# | ACN50232.1 |
| Expressed Host | HEK293 Cells |
| Species | H3N2 |
| Molecule Mass | The influenza H3N2 virus Neuraminidase comprises 424 amino acids. |
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: Comparison of immunogenicity of adjuvanted and high dose influenza vaccination in long-term care facility residents
authors: Didion Elise M.; Kass Joseph D.; ...; Canaday David H.
journal: medRxiv
date: 2024-10-15
cited_by_count: 0
techniques: Incubation; Inhibition; Recombinant
bioz_score: 92
title: Preparation of a thioxoimidazolidin-linked sialoside BSA conjugate for the inhibition of influenza virus.
authors: Haijuan Qin; Zhiwei Huang; ...; Yang Yang
journal: Carbohydrate Research
date: 2024-10-09
pmid: 39405815
doi: 10.1016/j.carres.2024.109287
cited_by_count: 0
techniques: Control; Mass Spectrometry; Mutagenesis; Recombinant; SPR Assay
bioz_score: 92
title: Improved influenza vaccine responses after expression of multiple viral glycoproteins from a single mRNA.
authors: Rebecca A Leonard; Kaitlyn N Burke; ...; Nicholas S Heaton
journal: Nature Communications
date: 2024-10-08
pmid: 39379405
cited_by_count: 13
techniques: Activity Assay; Control; In Vitro; Incubation; Positive Control; Recombinant
bioz_score: 92
title: A novel N -heterocycles substituted oseltamivir derivatives as potent inhibitors of influenza virus neuraminidase: discovery, synthesis and biological evaluation.
authors: Jiwei Zhang; Chuanfeng Liu; ...; Xinyong Liu
journal: Journal of enzyme inhibition and medicinal chemistry
date: 2023-11-14
pmid: 37955306
cited_by_count: 1
techniques: Incubation; Virus
bioz_score: 93
title: A mosaic influenza virus-like particles vaccine provides broad humoral and cellular immune responses against influenza A viruses
authors: Xuejie Liu; Tianyi Zhao; ...; Yuelong Shu
journal: NPJ vaccines
date: 2023-09-07
pmid: 37679361
doi: 10.1038/s41541-023-00728-5
pmcid: 10485063
cited_by_count: 23
techniques: Biomarker Discovery; Chromatin Immunoprecipitation; Control; Flow Cytometry; Magnetic Resonance Imaging; Virus
bioz_score: 92
title: Differential effects of specific cathepsin S inhibition in biocompartments from patients with primary Sjögren syndrome.
authors: Patrick Hargreaves; Douglas Daoudlarian; ...; Tobias Manigold
journal: Arthritis research & therapy
date: 2020-08-10
pmid: 31319889
cited_by_count: 18
techniques: Recombinant
bioz_score: 92
title: Inhibition of Influenza A Virus Infection by Fucoidan Targeting Viral Neuraminidase and Cellular EGFR Pathway
authors: Wei Wang; Jiandong Wu; ...; Guangli Yu
journal: Scientific Reports
date: 2017-01-17
pmid: 28094330
doi: 10.1038/srep40760
pmcid: 5240104
cited_by_count: 90
techniques: Activity Assay; Adsorption; Binding Assay; Electron Microscopy; Fluorescence; HI Assay; Hemagglutination Assay; Incubation; Infection; Inhibition; Labeling; Plaque Assay; Plasmid Preparation; Recombinant
bioz_score: 92
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