Rabbit anti-Human Influenza A Neuraminidase N1 Polyclonal Antibody | anti-H1N1 antibody

Influenza A Neuraminidase N1 (A/Georgia/20/2006) (H1N1) (PE)

Cat. Num. AAA6481631

• Reactivity: Human
• Applications: FLISA
• Purity: Purified by Immunoaffinity chromatography.
• Synonyms: Influenza A Neuraminidase N1; Polyclonal Antibody; Influenza A Neuraminidase N1 (A/Georgia/20/2006) (H1N1) (PE); anti-H1N1 antibody

• Host: Rabbit
• Reactivity: Human
• Clonality: Polyclonal
• Isotype: IgG
• Specificity: Recognizes the neuraminidase peptide from seasonal Influenza A (H1N1). Does not cross-react with the corresponding peptide from the swine-origin Influenza A/California/14/2009 (H1N1).
• Purity/Purification: Purified by Immunoaffinity chromatography.
• Form/Format: Supplied as a liquid in PBS, pH 7.2. No preservative added. No stabilizing proteins added. Labeled with R-Phycoerythrin (PE).

• Applicable Applications for anti-H1N1 antibody: FLISA
• Application Notes: Applications are based on unconjugated antibody.
• Immunogen: Synthetic peptide corresponding to the neuraminidase protein from seasonal Influenza A/Georgia/20/2006 (H1N1)
• Conjugate: PE
• Note: Preservative Free
• Preparation and Storage: Store product at 4 degree C in the dark. DO NOT FREEZE! Stable at 4 degree C for 12 months after receipt as an undiluted liquid. Dilute required amount only prior to immediate use. Further dilutions can be made in assay buffer. Caution: PE conjugates are sensitive to light. For maximum recovery of product, centrifuge the original vial prior to removing the cap.

ELISA (EIA)

(ELISA results at 1ug/ml and the blocking and corresponding peptides at 50, 10, 2 and 0ng.)

Related Product Information for anti-H1N1 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.

Product Categories/Family for anti-H1N1 antibody

Antibodies; Infectious Disease Influenza

References

1. Thompson, W.W., et al., (2003), "Mortality associated with influenza and respiratory syncytial virus in the United States, " JAMA, 289:179-186. 2. Dawood, F.S., et al., (2009), "Novel Swine-Origin Influenza A (H1N1) Virus Investigation Team, Emergence of a novel swine-origin influenza A (H1N1) virus in humans, " N. Engl. J. Med., 360:2605-2615. 3. Butler D., (2009), "Swine flu goes global, " Nature, 458:1082-1083. 4. Morens, D.M., et al., (2009), "The Persistent Legacy of the 1918 Influenza Virus, " N. Engl. J. Med., June 29. 5. Garten R.J., et al., (2009), "Antigenic and Genetic Characteristics of Swine-Origin 2009 A (H1N1) Influenza Viruses Circulating in Humans, " Science, May 22.

NCBI and Uniprot Product Information

• NCBI GI #: 168827347
• UniProt Accession #: B1AGS8
• Molecular Weight: 51,665 Da
• NCBI Official Full Name: neuraminidase
• UniProt Protein Name: Neuraminidase
• UniProt Gene Name: NA
• UniProt Entry Name: B1AGS8_9INFA

Uniprot Description

Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Otherwise, infection would be limited to one round of replication. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. May facilitate viral invasion of the upper airways by cleaving the sialic acid moities on the mucin of the airway epithelial cells. Likely to plays a role in the budding process through its association with lipid rafts during intracellular transport. May additionally display a raft-association independent effect on budding. Plays a role in the determination of host range restriction on replication and virulence. Sialidase activity in late endosome/lysosome traffic seems to enhance virus replication.