Hemagglutinin/HA Protein, H6N4 (CAC84244, sf9, His)

Hemagglutinin/HA protein attaches to sialic acid receptors, initiating virus binding to cells. This attachment prompts virion internalization via clathrin-dependent or -independent pathways. HA is pivotal in determining virus host range and virulence. As a Class I viral fusion protein, it facilitates virus entry into the cell cytoplasm by mediating fusion between the endocytosed virus particle's membrane and the endosomal membrane. In endosomes' low pH, HA2 undergoes an irreversible conformational change, releasing the fusion hydrophobic peptide. Multiple HA trimers are essential for forming a competent fusion pore. Hemagglutinin/HA Protein, H6N4 (CAC84244, sf9, His) is the recombinant Virus-derived Hemagglutinin/HA protein, expressed by Sf9 insect cells, with C-His labeled tag. The total length of Hemagglutinin/HA Protein, H6N4 (CAC84244, sf9, His) is 529 a.a., with molecular weight of ~52.6 KDa.

Hemagglutinin/HA protein binds to sialic acid-containing receptors on the cell surface, leading to the attachment of the virus particle to the cell. This attachment can trigger virion internalization through either clathrin-dependent endocytosis or a clathrin- and caveolin-independent pathway. HA protein plays a crucial role in determining the host range restriction and virulence of the virus. As a class I viral fusion protein, it is responsible for facilitating the penetration of the virus into the cell cytoplasm by mediating the fusion between the membrane of the endocytosed virus particle and the endosomal membrane. In the low pH environment of endosomes, HA2 undergoes an irreversible conformational change, which results in the release of the fusion hydrophobic peptide. Multiple HA trimers are required to form a competent fusion pore.

Virus

Sf9 insect cells

C-His

Q8UWX0 (M1-Q529)

/

Approximately 52.6 kDa.

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

<1 EU/μg, determined by LAL method.