Anti-Influenza B Neuraminidase [Clone B19]

Influenza B HK/73.

PBS, pH 7.4.

Liquid

Purified by Protein G affinity chromatography

This antibody is stable for at least one (1) year at -20°C to -70°C. Store product in appropriate aliquots to avoid multiple freeze-thaw cycles.

Next Day 2-8°C

Mouse Monoclonal Antibody specific to Influenza B Neuraminidase

Mechanism of Action: Influenza Neuraminidase
Neuraminidases are critical surface enzymes responsible for cleaving sialic acid groups from glycoproteins. In the context of the Influenza B virus, viral neuraminidase (NA) plays a pivotal role in the lifecycle of the pathogen. Structurally, Influenza neuraminidase is composed of four identical subunits arranged in a square tetramer, anchored to the virus surface by a long protein stalk. The enzyme’s active sites are located in deep depressions on the upper surface, where they bind to polysaccharide chains and clip off terminal sugars.

Neuraminidase vs. Hemagglutinin in Viral Infection
-Neuraminidase (NA) and Hemagglutinin (HA) are the two major membrane glycoproteins found on the surface of the influenza virus. They function in concert but with opposing roles:

- Hemagglutinin (HA): Initiates infection by binding to sialic acid-containing receptors on the surface of host cells.

- Neuraminidase (NA): Facilitates viral release. It acts as a receptor-destroying enzyme by cleaving the HA-sialic acid bond between newly formed virions and host cell receptors during budding.

Research Applications for Anti-Influenza B Neuraminidase Antibodies
Because of its essential role in viral spread, neuraminidase is a primary target for anti-influenza virus therapy development (such as neuraminidase inhibitors) and vaccine research. High-quality Influenza antibodies are indispensable tools for these studies.

This Anti-Influenza B Neuraminidase Antibody (Cat. No. 19601) is specifically designed to aid researchers in:
- Influenza Diagnosis: Detecting the presence of the Influenza B virus in biological samples.

- Vaccine Development: Characterizing viral strains and assessing the potency of neuraminidase antigens.

-Therapeutic Research: Screening and validating potential antiviral compounds that inhibit neuraminidase activity.

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 moieties 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. {HAMAP-Rule:MF_04071}.

G.M. Air et al. (1990) Virology 177: 578. (Catalog no. 19601 = MAb B3, 19602 = MAb B14, 19603 = MAb B19).