Anti-Seasonal and Swine H1N1 Neuraminidase antibody
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(1 Publication)
- ELISA
Unknown
ELISA - Anti-Seasonal and Swine H1N1 Neuraminidase antibody (AB91645)
ELISA using ab91645 at 1 μg/ml, detects 2 ng of free peptide (Seasonal and Swine H1N1 Neuraminidase).
- ELISA
Supplier Data
ELISA - Anti-Seasonal and Swine H1N1 Neuraminidase antibody (AB91645)
Validation with H1N1 NA Protein Coating Antigen : H1N1 Neuraminidase recombinant protein, 2 μg/mL, incubated at 4˚C overnight. Detection Antibodies : ab91645, dilution : 1-1000 ng/mL, incubated at RT for 1 hr. Secondary Antibodies : Goat anti-rabbit at 1/10000 dilution, incubated at RT for 1 hr.
- WB
Supplier Data
Western blot - Anti-Seasonal and Swine H1N1 Neuraminidase antibody (AB91645)
1h incubation at RT in 5% NFDM/TBST.
All lanes:
Western blot - Anti-Seasonal and Swine H1N1 Neuraminidase antibody (ab91645) at 2 µg/mL
Lane 1:
H1N1 Swine Neuraminidase recombinant protein at 50 ng
Lane 2:
H1N1 Swine Neuraminidase recombinant protein at 100 ng
false
Reactivity data
Properties and storage information
Form
Purification technique
Storage buffer
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
The neuraminidase protein acts as a sialidase catalyzing the hydrolysis of terminal sialic acid residues. This protein functions as part of a tetramer complex on the viral envelope where its activity complements that of hemagglutinin another surface protein. While hemagglutinin allows the virus to attach to the host cell by binding to sialic acid neuraminidase enables the virus to release and spread by cleaving these same residues post-replication. This balance between attachment and release is important for optimal viral propagation and infection cycle continuation.
Pathways
Neuraminidase activity intersects in the host cell pathways involved in glycan modification and processing. Neuraminidase contributes to the process known as glycan degradation where the removal of sialic acid groups modulates cell-surface molecule interactions. This protein and its functional counterpart hemagglutinin are central to the viral replication pathway and the overall influenza infection pathway. Both proteins coordinate their activities to ensure efficient viral entry and exit from host cells underpinning the infectious cycle of the virus.
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Publications (1)
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Virology journal 20:183 PubMed37596622
2023
Applications
Unspecified application
Species
Unspecified reactive species
Product promise
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