Recombinant Influenza A Virus H1N1 Neuraminidase Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 4858-NM

R&D Systems, part of Bio-Techne
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4858-NM-005
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Key Product Details

Source

Sf 21 (baculovirus)

Accession #

AAF77036

Conjugate

Unconjugated

Applications

Enzyme Activity

View all Viral Neuraminidase Proteins and Enzymes »

Product Specifications

Source

Spodoptera frugiperda, Sf 21 (baculovirus)-derived influenza a virus h1n1 Viral Neuraminidase protein
Ser37-Lys469, with an N-terminal 6-His tag

Purity

>80%, by SDS-PAGE under reducing conditions and visualized by silver stain.

Endotoxin Level

<1.0 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

His

Predicted Molecular Mass

48 kDa

SDS-PAGE

57 kDa, reducing conditions

Activity

Measured by its ability to cleave a fluorogenic substrate, 2’-(4-Methylumbelliferyl)-alpha -D-N-acetylneuraminic acid.
The specific activity is >2,500 pmol/min/µg, as measured under the described conditions.

Formulation, Preparation and Storage

4858-NM
Formulation Supplied as a 0.2 μm filtered solution in Tris, NaCl and Glycerol.
Shipping The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 3 months, -20 to -70 °C under sterile conditions after opening.

Background: Viral Neuraminidase

Neuraminidase (NA) and hemagglutinin (HA) are major membrane glycoproteins found on the surface of influenza virus. HA is a lectin that binds sialic acid on host cell membrane. NA is a sialic acid hydrolase that specifically clips off terminally located sialic acid on host cell surface. The two proteins are essential for the infectious cycle of the influenza virus. During initial infection, an influenza virus will hold onto an epithelial cell through HA-sialic acid interaction. At the end of an infectious cycle, the NA will cleave the sialic acid on the host cell membrane, releasing the formed viral particle from the HA-sialic acid bondage (1). The neuraminidase activity is also thought to help the virus penetrate mucus. Nine subtypes of NA have been identified, all of which are tetrameric and share a common structure consisting of a globular head, a thin stalk region, and a small hydrophobic region that anchors the protein in the virus membrane (2). The purified rvH1N1NA consists of amino acid residues 37 to 469 as deduced from the 1918 Spanish flu virus NA (A/Bervig_Mission/1/18) (3). It has a distinct N-glycan profile and is resistant to trypsin digestion (4).

References

  1. Palese, P. & Compans, R. W. (1976) J. Gen. Virol. 33:159.
  2. Colman, P. M. et al. (1983) Nature 303:41.
  3. Reid, A. (2000) Proc. Natl. Acad. Sci. USA 97:6785.
  4. Wu, Z.L. et al. (2009) Biochem. Biophys. Res. Comm. 379:749.

Long Name

Neuraminidase

Alternate Names

NANH

UniProt

AAF77036 (Viral)

Additional Viral Neuraminidase Products

Product Documents for Recombinant Influenza A Virus H1N1 Neuraminidase Protein, CF

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Product Specific Notices for Recombinant Influenza A Virus H1N1 Neuraminidase Protein, CF

For research use only

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