HA/Hemagglutinin Protein, H5N1 (Q692M2, HEK293, His)

HA/Hemagglutinin Protein binds sialic acid receptors, initiating virus attachment to cells. This binding prompts virion internalization through clathrin-dependent or -independent pathways. Essential for host range and virulence, it acts as a Class I viral fusion protein, mediating viral and endosomal membrane fusion. In endosomes, low pH triggers irreversible HA2 conformational change, releasing the fusion peptide. Multiple trimers are required for a functional fusion pore. HA/Hemagglutinin Protein, H5N1 (Q692M2, HEK293, His) is the recombinant Virus-derived HA/Hemagglutinin protein, expressed by HEK293, with C-His labeled tag. The total length of HA/Hemagglutinin Protein, H5N1 (Q692M2, HEK293, His) is 342 a.a., with molecular weight of ~38.2 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 virion internalization through either clathrin-dependent endocytosis or a clathrin- and caveolin-independent pathway. It 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 mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane, allowing the penetration of the virus into the cell cytoplasm. The low pH environment in endosomes causes an irreversible conformational change in HA2, leading to the release of the fusion hydrophobic peptide. Multiple trimers are necessary to form a competent fusion pore.

Virus

HEK293

C-His

Q692M2 (M1-R342)

/

Approximately 38.2 kDa

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

<1 EU/μg, determined by LAL method.