Product Overview
A DNA sequence encoding the Influenza A virus (A/Brisbane/02/2018 (H1N1)) hemagglutinin (translated amino acids of EPI1312566) (Met1-Ile530), termed as HA, was expressed with a polyhistidine tag at the C-terminus.
Molecular Weight
The recombinant hemagglutinin of the Influenza A virus (A/Brisbane/02/2018 (H1N1)) consists of 524 amino acids and predicts a molecular mass of 59.2 kDa. it migrates as an approximately 63.4 kDa band in SDS-PAGE under reducing conditions.
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
Alternative Names
Influenzavirus A; Influenza A virus; Influenza A virus H1N1; H1N1; IAV H1N1; IAV H1N1 Hemagglutinin; IAV H1N1 HA; H1N1 HA; H1N1 Hemagglutinin
Purity
> 95 % as determined by SDS-PAGE.
Buffer
Lyophilized from sterile PBS, pH 7.4. 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 H1N1; H1N1; IAV H1N1; IAV H1N1 Hemagglutinin; IAV H1N1 HA; H1N1 HA; H1N1 Hemagglutinin
Citations
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Subbramanian, RA; Basha, S; et al. Age-related changes in magnitude and diversity of cross-reactive CD4(+) T-cell responses to the novel pandemic H1N1 influenza hemagglutinin. HUMAN IMMUNOLOGY 71:957-963(2010).
Zhang, Y; Zhu, JP; et al. Glycosylation on Hemagglutinin Affects the Virulence and Pathogenicity of Pandemic H1N1/2009 Influenza A Virus in Mice. PLOS ONE 8:-(2013).
COA
Certificate of Analysis
