Anti-H7N 9 HA蛋白質 (HA1+HA2)
A H7N9 (A/Anhui/1/2013) HA / Hemagglutinin Protein Datasheet
A DNA sequence
Influenza A virus
(53.8+44.7) % as determined by SDS-PAGE
H7N 9 HA protein
< 1.0 EU per μg of the protein as determined by the
Samples are stable for up to twelve months from date of
Predicted N terminal:
Lyophilized from sterile PBS, pH 7.4.
DKICLGHHAV SNGTKVNTLT ERGVEVVNAT ETVERTNIPR ICSKGKRTVD
Store it under sterile conditions at -70℃ . It is recommended that
A hardcopy of COA with reconstitution instruction is
H7N9 is a subtype of Influenza
virus A. On April 1, 2013, the World Health Organization (WHO) first reported 3
human infections with a new influenza A (H7N9) virus in China . Since
then, additional cases have been reported. This new H7N9 virus is an avian
(bird) influenza (flu) virus. Influenza (flu) is a respiratory infection in
mammals and birds. The virus is divided into three main types (Influenza A, Influenza
B, and Influenza C), which are distinguished by differences in two major
internal proteins (hemagglutinin (HA) and neuraminidase (NA).
Influenza A is further divided
into subtypes based on differences in the membrane proteins hemagglutinin (HA)
and neuraminidase (NA), which are the most important targets for the immune
system. The notation HhNn is used to refer to the subtype comprising the hth
discovered Hemagglutinin (HA) protein and the nth discovered neuraminidase (NA)
protein. The influenza viral Hemagglutinin (HA) protein is a homo trimer with a
receptor binding pocket on the globular head of each monomer.
The influenza virus
Hemagglutinin (HA) protein is translated in cells as a single protein, HA0, or
hemagglutinin precursor protein. For viral activation, hemagglutinin precursor
protein (HA0) 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.
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