NA/Neuraminidase Protein, H1N1 (P03468, HEK293)

The NA/Neuraminidase Protein is an influenza virus surface enzyme that cleaves sialic acid residues. Inhibiting NA/Neuraminidase Protein is crucial for antiviral drugs. Targeting NA/Neuraminidase Protein can help prevent viral release, reduce viral spread, and potentially treat influenza infections. NA/Neuraminidase Protein, H1N1 (P03468, HEK293) is the recombinant Virus-derived NA/Neuraminidase protein, expressed by HEK293 , with tag free. The total length of NA/Neuraminidase Protein, H1N1 (P03468, HEK293) is 454 a.a., with molecular weight of ~50.1 kDa.

The NA/Neuraminidase Protein is responsible for catalyzing the removal of terminal sialic acid residues from viral and cellular glycoconjugates. It plays a crucial role in virus release by cleaving off the terminal sialic acids on the glycosylated HA during virus budding, facilitating virus release and aiding in virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure efficient spread of the progeny virus from cell to cell, allowing for multiple rounds of replication. Referred to as a receptor-destroying enzyme, it cleaves terminal sialic acid from cellular receptors, potentially facilitating viral invasion of the upper airways by cleaving the sialic acid moieties on the mucin of airway epithelial cells. It is likely involved in the budding process through its association with lipid rafts during intracellular transport and may also have a raft-association independent effect on budding. Furthermore, it plays a role 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

P03468 (M1-K454)

956530  [NCBI]

Approximately 50.1 kDa

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

<1 EU/μg, determined by LAL method.