|Recombinant H1N1 HA protein|
|0.2 μm filtered solution in PBS with 50 % HRP-protector, pH 7.4|
|Produced in rabbits immunized with purified, recombinant Influenza A virus H1N1 (Swine Flu 2009) Hemagglutinin extracellular domain. H1N1 Hemagglutinin / HA specific IgG was purified by Influenza A virus H1N1 Hemagglutinin / HA affinity chromatography, and conjugated with horseradish peroxidase (HRP).|
|H1N1 (A/California/04/2009) HA|
H1N1 (A/California/07/2009) HA
WB: 1-2 μg/mL
ELISA: This antibody can be used as a detection reagent in a H1N1 HA sandwich immunoassay (Catalog#SEK001) in combination with the mouse anti-H1N1 HA monoclonal antibody and recombinant H1N1 HA as the standard. The suggested concentration range for this detection is 1-4 μg/mL and should be titrated to determine the optimal concentration.
This antibody can be used as a detection reagent in a H1N1 HA sandwich immunoassay (Catalog#SEK001) in combination with the mouse anti-H1N1 HA monoclonal antibody and recombinant H1N1 HA as the standard. The suggested concentration range for this detection is 1-4 μg/mL and should be titrated to determine the optimal concentration.
|This antibody can be stored at 2℃-8℃ for twelve months without detectable loss of activity. Do not freeze !|
The influenza viral Hemagglutinin (HA) protein is a homo trimer 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 host endosomal membrane with the viral membrane.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.