Product Overview
Recombinant Influenza A Virus H3N2 Neuraminidase antigen, was expressed in Spodoptera frugiperda, Sf21 (baculovirus). Ala46-Ile469, with an N-terminal CD33 signal, vasodilator-stimulated phophoprotein tetramerization domain and a C-terminal 6-His tag(Acce
Purity
> 85%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie. Blue stain at 5 μg per lane.
Storage
2-8°C short term, -20°C long term
Introduction
Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Otherwise, infection would be limited to one round of replication. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. May facilitate viral invasion of the upper airways by cleaving the sialic acid moities on the mucin of the airway epithelial cells. Likely to plays a role in the budding process through its association with lipid rafts during intracellular transport. May additionally display a raft-association independent effect on budding. Plays a role in the determination of host range restriction on replication and virulence. Sialidase activity in late endosome/lysosome traffic seems to enhance virus replication.
Antigen Description
Neuraminidase (NA) and hemagglutinin (HA) are the two predominant membrane glycoproteins found on the surface of an influenza virus particle. They are essential for the infectious cycle of the virus. HA recognizes and binds to the sialic acid on the host cell membrane to initiate a viral infection. NA cleaves the sialic acid at the end of the cycle, allowing the progeny virus to leave the host thus initiating the next round of infection. In the early stage of an infection, NA may also assist in viral penetration of the mucus layer in the airway of a host. Nine subtypes of NA (N1 to N9) have been identified, all of which are believed to be tetrameric and sharea basic structure consisting of a globular head, a thin stalk region, and a small hydrophobic region that anchors the protein in the virus membrane. Glycosylation is also found to be important for the stability and activity of these enzymes. Due to their critical role in the infectious cycle of a virus, influenza viral neuraminidasesare frequently used as targets for drug design. Both the anti-influenza drugs Tamiflu and Relenza are neuraminidase inhibitors. According to a recent structure determination, neuraminidases from influenza type A viruses form two genetically distinct groups, with the N1 and N2 neuraminidases representing each of the twogroups.
Keywords
NA; IAV NA; Influenza A Virus Neuraminidase; Influenza A NA; H3N2 Neuraminidase; H3N2; Neuraminidase
Citations
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