Influenza A H1N1 Neuraminidase / NA (N295S mutation) (Active)


Influenza A H1N1 Neuraminidase / NA (N295S mutation) (Active): Product Information

Measured by its ability to cleave a fluorogenic substrate, 2'-(4-Methylumbelliferyl)-α-D-N-acetylneuraminic acid.
The specific activity is > 800 U.
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/California/04/2009 (H1N1)) neuraminidase (ACP41107.1) (Met 1-Lys 469) was expressed, the cell lysates are collected, and bio-activity was tested. There is an amino acid change from Asparagine to Serine (N295S mutation) in NA / Neuraminidase.
Expressed Host
HEK293 Cells
Molecule Mass
The recombinant influenza A H1N1 Neuraminidase comprises 469 amino acids and has a predicted molecular mass of 52 kDa.
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.
Stability & Storage
It is recommended that 1 ml sterile water be added to the vial to prepare a stock solution.

Influenza A H1N1 Neuraminidase / NA (N295S mutation) (Active): Synonyms

NA Protein, H1N1

Neuraminidase/NA Background Information

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.
  • Sardet C., et al.,(1989), Molecular cloning, primary structure, and expression of the human growth factor-activatable Na+/H+ antiporter. Cell 56:271-280.
  • Sardet C., et al., (1990), Growth factors induce phosphorylation of the Na+/H+ antiporter, glycoprotein of 110 kD.Science 247:723-726.
  • 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.

H1N1 Neuraminidase/NA Proteins

H3N2 Neuraminidase/NA Proteins
