Influenza A H1N1 (A/California/07/2009) Neuraminidase / NA Protein (ECD, His Tag) sinobiological 40954-V08B

$739.00
In stock
SKU
40954-V08B
Catalog No.SizePrice (USD)
40954-V08B-100100 µg$765.73

General Information

FormulationLyophilized from sterile 20mM Tris, 300mM NaCl, 10% glycerol, pH 7.5. 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 protein as determined by the LAL method.
ShippingIn 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 & StorageSamples 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.
ReconstitutionTo 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.
ActivityMeasured by its ability to cleave a fluorogenic substrate, 2'-(4-Methylumbelliferyl)-α-D-N-acetylneuraminic acid.
Protein ConstructionA DNA sequence encoding the Influenza A virus (A/California/07/2009 (H1N1)) Neuraminidase / NA (EPI185379) (Ile30-Lys469) was expressed with a vasodilator-stimulated phosphoprotein tetramerization domain at the N-terminus and a polyhistidine tag at the C-terminus.
Accession#EPI185379
Expressed HostBaculovirus-Insect Cells
SpeciesH1N1
Predicted N TerminalAsp
Molecule MassThe recombinant NA subunit of the Influenza A virus (A/California/07/2009(H1N1)) consists 486 amino acids and predicts a molecular mass of 54.28 kDa. It migrates as an approximately 63.24 kDa band in SDS-PAGE under reducing conditions.

Image / Experimental Information

Image 1 Alt TextH1N1 Neuraminidase/NA Protein 36707
Image 1 URLSource image

Background Information

DescriptionNeuraminidases 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
  1. Sardet C., et al. ,(1989), Molecular cloning, primary structure, and expression of the human growth factor-activatable Na+/H+ antiporter. Cell 56:271-280.
  2. Sardet C., et al. , (1990), Growth factors induce phosphorylation of the Na+/H+ antiporter, glycoprotein of 110 kD.Science 247:723-726.
  3. Tse C.-M., et al. ,(1991), Molecular cloning and expression of a cDNA encoding the rabbit ileal villus cell basolateral membrane Na+/H+ exchanger.EMBO J. 10:1957-1967.

title: Redirecting NEU (neuraminidase) antigen to autophagosomes confers enhanced cross-reactive T-cell immunity against heterosubtypic influenza virus infection.
authors: Zirong Han; Weiqi Pan; ...; Caijun Sun
journal: Autophagy
date: 2026-07-07
pmid: 41655133
doi: 10.1080/15548627.2026.2629285
cited_by_count: 1
techniques: Enzyme-linked Immunosorbent Assay; Recombinant
bioz_score: 94

title: A combinatorial DNA vaccine encoding APC-targeted, bivalent HA and NA antigens results in an improved influenza vaccine.
authors: Ina Charlotta Werninghaus; Daniëla Maria Hinke; ...; Ranveig Braathen
journal: Journal of Immunology (Baltimore, Md. : 1950)
date: 2026-03-07
pmid: 41764724
doi: 10.1093/jimmun/vkaf378
cited_by_count: 0
techniques: Binding Assay; Control; Electroporation; Enzyme-linked Immunosorbent Assay; In Vivo; Injection; Produced; Virus
bioz_score: 94

title: Characteristics of neuraminidase-specific immune responses in influenza vaccinated or naturally infected populations in Shenzhen, China.
authors: Lisha Deng; Xueying Fan; ...; Caijun Sun
journal: Vaccine
date: 2025-11-10
pmid: 41218569
doi: 10.1016/j.vaccine.2025.127918
cited_by_count: 0
techniques: Enzyme-linked Immunosorbent Assay; Recombinant
bioz_score: 94

title: Lab-on-a-graphene-FET detection of key molecular events underpinning influenza virus infection and effect of antiviral drugs
authors: Ono T.; Kamada K.; ...; Matsumoto K.
journal: bioRxiv
date: 2020-03-20
doi: 10.1101/2020.03.18.996884
cited_by_count: 0
techniques: Binding Assay; Derivative Assay; Inhibition; Recombinant
bioz_score: 94

title: Development of a Point-of-Care Diagnostic for Influenza Detection with Antiviral Treatment Effectiveness Indication
authors: Richard C. Murdock; Karen M. Gallegos; ...; Ian Papautsky
journal: Lab on a Chip
date: 2018-01-17
pmid: 27966711
pmcid: 5241167
cited_by_count: 6
techniques: Negative Control; Purification
bioz_score: 94

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