Avian Influenza Neuraminidase Antibody is affinity chromatography purified via peptide column.
Immunogène
Avian influenza neuraminidase antibody was raised against a synthetic peptide corresponding to 15 amino acids near the carboxy terminus of the avian influenza neuraminidase protein. Efforts were made to use relatively conserved regions as the antigen. The immunogen is located within the last 50 amino acids of Avian Influenza Neuraminidase.
NA
Reactivité: Influenza B Virus
ELISA, Neut
Hôte: Souris
Monoclonal
B14
unconjugated
Indications d'application
Avian influenza neuraminidase antibody can be used for the detection of the avian influenza neuraminidase protein from the H5N1 strain of Avian influenza A in ELISA. It will detect 10 ng of free peptide at 1 μ,g/mL.
Restrictions
For Research Use only
Format
Liquid
Concentration
1 mg/mL
Buffer
Avian Influenza Neuraminidase Antibody is supplied in PBS containing 0.02 % sodium azide.
Agent conservateur
Sodium azide
Précaution d'utilisation
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Stock
-20 °C,4 °C
Stockage commentaire
Avian Influenza Neuraminidase antibody can be stored at 4°C for three months and -20°C, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.
Avian Influenza Neuraminidase Antibody: Influenza A virus is a major public health threat, killing more than 30,000 people per year in the USA. Novel influenza virus strains emerge periodically to which humans have little or no immunity, resulting in devastating pandemics. Influenza A can exist in a variety of animals, however it is in birds that all subtypes can be found. These subtypes are classified based on the combination of the virus coat glycoproteins hemagglutinin (HA) and neuraminidase (NA) subtypes. During 1997, an H5N1 avian influenza virus was determined to be the cause of death in 6 of 18 infected patients in Hong Kong. There was some evidence of human to human spread of this virus, but it is thought that the transmission efficiency was fairly low. Although it has been known that cleavage site and glycosylation patterns of the HA protein play important roles in determining the pathogenicity of H5 avian influenza viruses, it has only recently been shown that an additional glycosylation site within the globular head of the NA protein also contributes to the high virulence of the H5N1 virus.