HA/Hemagglutinin Protein, H9N1 (Q20PC1, sf9, His)

The Hemagglutinin HA1 protein is pivotal for attaching virus particles to host cells through binding to sialic acid-containing receptors, inducing virion internalization via clathrin-dependent or clathrin- and caveolin-independent pathways. As a Class I viral fusion protein, HA1 determines host range restriction and virulence, mediating fusion between the virus particle's membrane and the endosomal membrane. The low pH in endosomes triggers an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Cooperative trimer action forms a competent fusion pore, highlighting HA1's intricate role in viral entry. HA/Hemagglutinin Protein, H9N1 (Q20PC1, sf9, His) is the recombinant Virus-derived HA/Hemagglutinin protein, expressed by Sf9 insect cells, with C-His labeled tag. The total length of HA/Hemagglutinin Protein, H9N1 (Q20PC1, sf9, His) is 523 a.a., with molecular weight of ~58.1 kDa.

The Hemagglutinin HA1 protein is instrumental in the attachment of virus particles to host cells by binding to sialic acid-containing receptors on the cell surface. This attachment triggers virion internalization through either clathrin-dependent endocytosis or a clathrin- and caveolin-independent pathway. HA1 plays a crucial role in determining host range restriction and virulence, functioning as a Class I viral fusion protein that facilitates the penetration of the virus into the cell cytoplasm by mediating the fusion of the endocytosed virus particle's membrane with the endosomal membrane. The low pH environment in endosomes induces an irreversible conformational change in HA2, leading to the release of the fusion hydrophobic peptide. The formation of a competent fusion pore requires the cooperative action of several trimers, underscoring the intricate mechanisms by which HA1 contributes to viral entry and infection.

Virus

Sf9 insect cells

C-His

Q20PC1 (M1-K523)

/

Approximately 58.1 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.