HA/Hemagglutinin Protein, H5N1 (G2U0T8, HEK293, His)

HA/Hemagglutinin Protein binds to sialic acid receptors, initiating virus attachment to cells. Internalization occurs through clathrin-dependent or -independent pathways. HA crucially influences host range and virus virulence. As a Class I viral fusion protein, it mediates membrane fusion between the endocytosed virus particle and the endosomal membrane, enabling virus entry into the cell cytoplasm. In low pH endosomes, HA2 undergoes an irreversible conformational change, releasing the fusion hydrophobic peptide. Multiple HA trimers are necessary for a competent fusion pore. HA/Hemagglutinin Protein, H5N1 (G2U0T8, 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 (G2U0T8, HEK293, His) is 530 a.a., with molecular weight of 65-70 kDa.

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

Virus

HEK293

C-His

G2U0T8 (M1-Q530)

/

65-70 kDa

Greater than 90% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.