Rabbit anti-Virus H1N1 Neuraminidase Polyclonal Antibody | anti-NA antibody

H1N1 Neuraminidase Antibody

Cat. Num. AAA151366

• Reactivity: Virus
• Applications: ELISA
• Purity: H1N1 Neuraminidase Antibody is affinity chromatography purified via peptide column.
• Synonyms: H1N1 Neuraminidase; Polyclonal Antibody; H1N1 Neuraminidase Antibody; neuraminidase / neuraminidase; anti-NA antibody

• Host: Rabbit
• Reactivity: Virus
• Clonality: Polyclonal
• Isotype: IgG
• Specificity: This antibody will recognize the Neuraminidase from the both the seasonal influenza (H1N1) and swine-origin influenza virus (A/California/14/2009 (H1N1)).
• Purity/Purification: H1N1 Neuraminidase Antibody is affinity chromatography purified via peptide column.
• Form/Format: Liquid
• Concentration: 1 mg/mL (varies by lot)
• Sequence Length: 470

• Applicable Applications for anti-NA antibody: ELISA (EIA)
• Application Notes: Neuraminidase antibody can be used for the detection of the Neuraminidase protein from the seasonal influenza A (H1N1) and the novel swine influenza in ELISA. It will detect 2 ng of free peptide at 1 mug/mL.
• Conjugate: Unconjugated
• Immunogen: Neuraminidase antibody was raised against synthetic peptides from. The seasonal influenza (H1N1) Neuraminidase protein and the novel swine influenza Neuraminidase protein.; ; The antibody recognizes both variants.
• Buffer: H1N1 Neuraminidase Antibody is supplied in PBS containing 0.02% sodium azide.
• Preparation and Storage: H1N1 Neuraminidase antibody can be stored at 4 degree C for three months and -20 degree 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.

ELISA (EIA)

(ELISA results using H1N1 Neuraminidase antibody at 1 μg/mL and the blocking and corresponding peptides at 50, 10, 2 and 0 ng/mL.)

Related Product Information for anti-NA antibody

H1N1 Neuraminidase Antibody: Influenza A virus is a major public health threat, killing more than 30, 000 people per year in the USA. In early 2009, a novel swine-origin influenza A (H1N1) virus was identified in specimens obtained from patients in Mexico and the United States. The virus spread quickly around the world and on June 11, 2009, the World Health Organization declared it a pandemic. Influenza A virus has one of sixteen possible Hemagglutinin (HA) surface proteins and one of nine possible Neuraminidase (NA) surface proteins. The Hemagglutinin protein facilitates viral attachment while Neuraminidase is involved in viral release. These proteins also elicit immune responses that prevent infection or independently reduce viral replication. The genetic make-up of this swine flu virus is unlike any other: it is an H1N1 strain that combines a triple assortment first identified in 1998 including human, swine, and avian influenza with two new pig H3N2 virus genes from Eurasia, themselves of recent human origin. The distinct antigenic properties of the new swine influenza virus compared with seasonal influenza A (H1N1) virus suggest that human immunity against new swine influenza virus is limited, although the age distribution of reported cases suggests some degree of protection in older age groups.

NCBI and Uniprot Product Information

• NCBI GI #: 168827347
• UniProt Accession #: B1AGS8; C4AL28
• Molecular Weight: 51,665 Da
• NCBI Official Full Name: neuraminidase
• UniProt Protein Name: Neuraminidase
• Protein Family: 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.