NA/Neuraminidase Protein, H1N1 (P03469, HEK293)

NA/Neuraminidase Protein, an enzyme found on the surface of influenza viruses, is responsible for the cleavage of sialic acid residues. Inhibition of NA/Neuraminidase Protein is a key target for antiviral drugs. Targeting NA/Neuraminidase Protein may provide potential therapeutic interventions by preventing viral release, reducing viral spread, and potentially treating influenza infections. NA/Neuraminidase Protein, H1N1 (P03469, HEK293) is the recombinant Virus-derived NA/Neuraminidase protein, expressed by HEK293 , with tag free. The total length of NA/Neuraminidase Protein, H1N1 (P03469, HEK293) is 470 a.a., with molecular weight of ~51.9 kDa.

The NA/Neuraminidase protein acts as a catalyst in removing sialic acid residues from viral and cellular glycoconjugates. It plays a crucial role in virus budding by cleaving off terminal sialic acids on the glycosylated HA, aiding in the release of the virus. Additionally, it facilitates virus spread by further removing sialic acids from the cell surface, preventing self-aggregation and ensuring efficient spread from cell to cell. This protein is referred to as a receptor-destroying enzyme as it cleaves terminal sialic acids from cellular receptors. It may also contribute to viral invasion of the upper airways by cleaving sialic acid moieties on the mucin of airway epithelial cells. NA is associated with lipid rafts during intracellular transport, potentially aiding in the budding process, and may have raft-association independent effects as well. It is involved in determining host range restriction on replication and virulence, and its sialidase activity in late endosome/lysosome traffic appears to enhance virus replication.

Virus

HEK293

Tag Free

P03469 (M1-K470)

/

Approximately 51.9 kDa

Greater than 80% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.