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> Enzymes > Neuraminidase (NA) > Influenza A H5N1 Neuraminidase / NA ( H274Y ) (Active) Influenza A H5N1 Neuraminidase / NA ( H274Y ) (Active)
| Catalog | Size (Price) | Quantity | In Stock | Operation | Other Information |
| 11676-VNAHC1 |
|
YES |
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Influenza A Virus H5N1 NA / Neuraminidase ( H274Y ) ( Lyophilized )
H5N1 NA / Neuraminidase ( H274Y ) Price Inquiry
- Bulk Order: Inquiring Price
H5N1 NA / Neuraminidase ( H274Y ) Product Information
| Synonym : |
NA |
| Protein Construction: |
A DNA sequence encoding the Influenza A virus (A/Anhui/1/2005 (H5N1)) neuraminidase (ABU94738.1) (Met 1-Lys 449) was expressed, the cell lysates are collected, and bio-activity was tested |
| Source: | Influenza A Virus H5N1 |
| Expression Host: | Human Cells |
H5N1 NA / Neuraminidase ( H274Y ) QC Testing
| Purity: | N / A |
| Bio-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℃. |
| Stability: | Samples are stable for up to twelve months from date of receipt at -70℃ |
| Molecular Mass: |
The recombinant influenza A H5N1 Neuraminidase comprises 450 amino acids and has a predicted molecular mass of 49.2 kDa |
| Formulation: | Lyophilized from PBS, 0.6% Triton X-100, 7% Trehalose, 6% Mannitol, pH7.4 Please contact us for any concerns or special requirements. |
H5N1 NA / Neuraminidase ( H274Y ) Usage Guide
| Storage: | Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles. |
| Reconstitution: |
It is recommended that 1 ml sterile water be added to the vial to prepare a stock solution. |
H1N1 NA / Neuraminidase ( H274Y ) Related Products & Topics
Related Areas:
Enzyme>>Carbohydrate Metabolism Enzymes>>H5N1 neuraminidase/H1N1 NA
Immunology>>Innate Immunity>>Lysosomal Enzyme>>H5N1 neuraminidase/H1N1 NA
Virus>>Influenza Virus>>H5N1 neuraminidase/H1N1 NA
Proteins:
| Products | Source (CLICK for detailed Info. and Price) | Molecule | Description | Cat No |
| Protein | Influenza H5N1 Neuraminidase(NA)![]() |
NA | - | 11676-VNAHC |
| Protein | Influenza H5N1 Neuraminidase(NA)![]() |
NA | - | 11676-VNAHC1 |
Antibodies:
Related Influenza Virus Research Tools
H5N1 NA / Neuraminidase Description
Neuraminidase (NA) is a major membrane glycoproteins found on the surface of influenza virus. NA specifically catalyzes the hydrolysis removal of terminal sialic acid residues from viral and cellular glycoconjugates. It is known that HA binds to the sialic acid-containing receptors on the surface of host cells during initial infection, and at the end of an infectious cycle, NA cleaves the HA-sialic acid bondage from the newly formed virions and the host cell receptors during budding. NA thus is described as a receptor-destroying enzyme which facilitates virus release and efficient spread of the progeny virus from cell to cell. NA is a single-pass type I I membrane protein which exists as a homotetramer, and the transmembrane domain is involved in lipid raft association during intracellular transport. NA is suggested to play a role in the determination of host range restriction on replication and virulence. Nine subtypes of NA have been identified, and subtypes N1 and N2 have been positively linked to epidemics in man.
Influenza A virus subtype H5N1, also known as "bird flu", A(H5N1) or simply H5N1, is a subtype of the Influenza A virus which can cause illness in humans and many other animal species. H5N1 is easily transmissible between birds facilitating a potential global spread of H5N1. It is mainly spread by domestic poultry, both through the movements of infected birds and poultry products and through the use of infected poultry manure as fertilizer or feed. Humans with H5N1 have typically caught it from chickens, which were in turn infected by other poultry or waterfowl.
References
- Barman, S. et al., 2000, J. Virol. 74: 6538-45.
- Colman, P.M. et al., 1983, Nature. 303: 41-4.
- Suzuki, T. et al., 2005, J. Virol. 79: 11705-15.
- Shinya K, et al., 2006, Nature. 440 (7083): 435-6.
- von, Itzstein, M. 2007, Nat. Rev. Drug. Discov. 6: 967-74.
- Christophe F, et al., 2009, Science. 324:1557-61.
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