Influenza A H1N1 (Swine Flu 2009) Hemagglutinin / HA Antibody (HRP), Rabbit PAb, Antigen Affinity Purified

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Influenza A H1N1 (Swine Flu 2009) Hemagglutinin / HA Antibody (HRP), Rabbit PAb, Antigen Affinity Purified (Rabbit Polyclonal antibody) General Information

Product name
Influenza A H1N1 (Swine Flu 2009) Hemagglutinin / HA Antibody (HRP), Rabbit PAb, Antigen Affinity Purified
Validated applications
WB,ELISA(Det) (Antibody's applications have not been validated with corresponding viruses. Optimal concentrations/dilutions should be determined by the end user.)
Specificity
Influenza Hemagglutinin / HA
Immunogen
Recombinant H1N1 HA protein
Preparation
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).
Source
Polyclonal Rabbit IgG
Purification
Protein A & Antigen Affinity
Formulation
0.2 μm filtered solution in PBS with 50 % HRP-protector, pH 7.4
Conjugate
HRP
Form
Liquid
Shipping
This antibody is shipped as liquid solution at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Storage
This antibody can be stored at 2℃-8℃ for twelve months without detectable loss of activity. Protected from prolonged exposure to light. Do not freeze !

Influenza A H1N1 (Swine Flu 2009) Hemagglutinin / HA Antibody (HRP), Rabbit PAb, Antigen Affinity Purified (Rabbit Polyclonal antibody) Validated Applications

Application Dilution
WB his antibody can be used at 1:500-1:1000 to detect H1N1 HA. The detection limit for H1N1 HA is approximately 3 ng/lane and 6 ng/lane under reducing and Non-reducing conditions.
ELISA(Det)
Notes
ELISA(Det): 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.
Please Note: Optimal concentrations/dilutions should be determined by the end user.

Hemagglutinin / HA Background Information

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, 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.
Full Name
Harvey rat sarcoma viral oncogene homolog
References
  • White JM, Hoffman LR, Arevalo JH, et al. (1997). ""Attachment and entry of influenza virus into host cells. Pivotal roles of hemagglutinin"". In Chiu W, Burnett RM, Garcea RL. Structural Biology of Viruses.
  • Suzuki Y (March 2005). ""Sialobiology of influenza: molecular mechanism of host range variation of influenza viruses"". Biol. Pharm. Bull. 28 (3): 399–408.
  • Senne DA, Panigrahy B, Kawaoka Y, et al. (1996). ""Survey of the hemagglutinin (HA) cleavage site sequence of H5 and H7 avian influenza viruses: amino acid sequence at the HA cleavage site as a marker of pathogenicity potential"". Avian Dis. 40 (2): 425–37
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