HA/Hemagglutinin Protein, H5N1 (Q207Z6, sf9, His)

The HA/Hemagglutinin Protein attaches to sialic acid receptors, initiating virus internalization via clathrin-dependent or -independent pathways. It crucially determines host range and virulence, mediating fusion between the endocytosed virus particle's membrane and the endosomal membrane as a Class I viral fusion protein. In the low pH endosome environment, HA2 undergoes an irreversible conformational change, releasing the fusion hydrophobic peptide. Multiple HA trimers are essential for a competent fusion pore. Its roles in receptor binding, internalization, fusion, and membrane penetration shape viral characteristics. HA/Hemagglutinin Protein, H5N1 (Q207Z6, 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, H5N1 (Q207Z6, sf9, His) is 531 a.a., with molecular weight of ~60.1 kDa.

The HA/Hemagglutinin Protein binds to sialic acid-containing receptors on the cell surface, facilitating the attachment of the virus particle to the cell. This attachment triggers the internalization of the virion either through clathrin-dependent endocytosis or a clathrin- and caveolin-independent pathway. It plays a significant role in determining the host range restriction and virulence of the virus. As a class I viral fusion protein, it is responsible for mediating the fusion of the endocytosed virus particle's membrane with the endosomal membrane, allowing the virus to enter the cell cytoplasm. In the low pH environment of endosomes, the HA2 undergoes an irreversible conformational change, resulting in the release of the fusion hydrophobic peptide. Multiple HA trimers are necessary to form a competent fusion pore.

Virus

Sf9 insect cells

C-His

Q207Z6 (M1-Q531)

/

Approximately 60.1 kDa

Greater than 95% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.