NA/Neuraminidase Protein, H1N2 (QAX25989, HEK293, His)

NA/Neuraminidase Protein is a receptor-destroying enzyme that cleaves terminal sialic acids from cellular receptors, potentially facilitating viral invasion of the upper airways by targeting sialic acid moieties on airway epithelial cell mucin.NA plays a pivotal role in viral propagation by catalyzing the removal of terminal sialic acid residues from both viral and cellular glycoconjugates.Moreover, the sialidase activity in late endosome/lysosome traffic appears to enhance virus replication.NA/Neuraminidase Protein, H1N2 (QAX25989, HEK293, His) is the recombinant Virus-derived NA/Neuraminidase protein, expressed by HEK293 , with N-His labeled tag.

Neuraminidase (NA) plays a pivotal role in viral propagation by catalyzing the removal of terminal sialic acid residues from both viral and cellular glycoconjugates. Specifically, during virus budding, NA cleaves off terminal sialic acids from the glycosylated hemagglutinin (HA), facilitating the release of viral particles and enabling efficient virus spread through the circulation. By preventing self-aggregation and ensuring the removal of sialic acids from the cell surface, NA allows the progeny virus to disseminate efficiently from cell to cell, thereby avoiding limitations to a single round of replication. Described as a receptor-destroying enzyme, NA cleaves terminal sialic acids from cellular receptors, potentially facilitating viral invasion of the upper airways by targeting sialic acid moieties on airway epithelial cell mucin. Its association with lipid rafts during intracellular transport, and its potential raft-independent effect on budding, highlight the multifaceted role of NA in determining host range restriction, replication, and virulence. Moreover, the sialidase activity in late endosome/lysosome traffic appears to enhance virus replication^[1][2][3].

Virus

HEK293

N-His

QAX25989 (H36-I469)

/

Approximately 50.7 kDa

Greater than 85% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.