Product Overview
A DNA sequence encoding the Influenza A H3N2 (A/Hong Kong/4801/2014) Hemagglutinin (EPI653201) (Met1-Trp530) was expressed with a polyhistidine tag at the C-terminus.
Molecular Weight
The recombinant heterodimer of Influenza A H3N2 (A/Hong Kong/4801/2014) Hemagglutinin consists of 525 amino acids and has a calculated molecular mass of 59.26 KDa.
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
Alternative Names
Influenzavirus A; Influenza A virus; Influenza A virus H3N2; H3N2; IAV H3N2; IAV H3N2 Hemagglutinin; IAV H3N2 HA; H3N2 HA; H3N2 Hemagglutinin
Purity
> 95 % as determined by SDS-PAGE.
Buffer
Lyophilized from sterile 20mM PBS, pH 7.0, 150mM NaCl, 10% glycerol. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.
Storage
Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Introduction
The influenza viral Hemagglutinin (HA) protein is a homotrimer with a receptor binding pocket on the globular head of each monomer.HA has at least 18 different antigens. These subtypes are named H1 through H18.HA has two functions. Firstly, it allows the recognition of target vertebrate cells, accomplished through the binding to these cells' sialic acid-containing receptors. Secondly, once bound it facilitates the entry of the viral genome into the target cells by causing the fusion of the host endosomal membrane with the viral membrane. The influenza virus Hemagglutinin (HA) protein is translated in cells as a single protein, HA, or hemagglutinin precursor protein. For viral activation, hemagglutinin precursor protein (HA) must be cleaved by a trypsin-like serine endoprotease at a specific site, normally coded for by a single basic amino acid (usually arginine) between the HA1 and HA2 domains of the protein. After cleavage, the two disulfide-bonded protein domains produce the mature form of the protein subunits as a prerequisite for the conformational change necessary for fusion and hence viral infectivity.
Keywords
Influenzavirus A; Influenza A virus; Influenza A virus H3N2; H3N2; IAV H3N2; IAV H3N2 Hemagglutinin; IAV H3N2 HA; H3N2 HA; H3N2 Hemagglutinin
Citations
Publication ()
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COA
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