HA/Hemagglutinin Protein, H3N2 (Q91MA7, HEK293, His)

HA/Hemagglutinin Protein binds to sialic acid receptors on the cell surface, facilitating virus particle attachment and triggering virion internalization through clathrin-dependent or -independent pathways. HA plays a crucial role in host range determination and virus virulence. As a Class I viral fusion protein, it mediates the fusion of the endocytosed virus particle's membrane with the endosomal membrane, allowing virus entry into the cell cytoplasm. The acidic endosomal environment induces a permanent conformational change in HA2, releasing the fusion hydrophobic peptide. Multiple HA trimers are essential for forming a competent fusion pore. HA is a homotrimer with disulfide-linked HA1-HA2 subunits. HA/Hemagglutinin Protein, H3N2 (Q91MA7, 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, H3N2 (Q91MA7, HEK293, His) is 524 a.a., with molecular weight of ~57.2 kDa.

The Hemagglutinin Protein (HA) 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. HA 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 penetrating the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. The acidic environment in endosomes causes a permanent change in the conformation of HA2, leading to the release of the fusion hydrophobic peptide. Multiple trimers of HA are necessary to form a competent fusion pore. HA exists as a homotrimer, with disulfide-linked HA1-HA2 subunits.

Virus

HEK293

C-His

Q91MA7 (M1-S524)

/

Approximately 57.2 kDa

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

<1 EU/μg, determined by LAL method.