Flu-8Am Aat Bioquest Sharps Container (Medium) Covidien 8980S Flu-8Am Aat Bioquest

Description: A polyclonal antibody for detection of AAT from Human. This AAT antibody is for WB, IHC-P, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from the N-terminal region of human AAT

Description: A Rabbit Polyclonal antibody against AAT from Human. This antibody is tested and validated for WB, ELISA, IHC, WB, ELISA

Description: A Rabbit Polyclonal antibody against AAT from Human. This antibody is tested and validated for WB, ELISA, IHC, WB, ELISA

Description: A Rabbit Polyclonal antibody against AAT from Human. This antibody is tested and validated for WB, ELISA, IHC, WB, ELISA

Description: A Rabbit Polyclonal antibody against AAT from Human. This antibody is tested and validated for WB, ELISA, IHC, WB, ELISA

Description: Mouse Monoclonal to AAT

Description: Rabbit polyclonal to AAT.

Description: Rabbit polyclonal to AAT.

Description: Mouse monoclonal to AAT.

Description: Mouse monoclonal to AAT.

Description: 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 neuraminidase protein also contributes to the high virulence of the H5N1 virus. H5N1 hemagglutinin interacts with cell surface proteins containing oligosaccharides with terminal sialyl residues. Virus isolated from a human infected with the H5N1 strain in 1997 could bind to oligosaccharides from human as well as avian sources, indicating its species-jumping ability.;;For images please see PDF data sheet