Recombinant Human Neuraminidase protein (His tag N-Terminus)
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Recombinant Human Neuraminidase protein (His tag N-Terminus) is a Human Full Length protein, in the 48 to 415 aa range, expressed in Escherichia coli, with >85%, suitable for SDS-PAGE, Mass Spec.
View Alternative Names
NANH, NEU1, Sialidase-1, Acetylneuraminyl hydrolase, G9 sialidase, Lysosomal sialidase, N-acetyl-alpha-neuraminidase 1
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human Neuraminidase protein (His tag N-Terminus) (AB131685)
15% SDS-PAGE analysis of 3 µg ab131685.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Neuraminidase significantly impacts viral virulence and host cell infection. It is part of the functional machinery required for viral particle detachment from the host cell membrane facilitating the spread of infection. Neuraminidase works alongside other viral proteins including hemagglutinin which attaches the virus to the host cell. The neuraminidase function of trimming sialic acids is critical in the ongoing interaction between virus and host.
Pathways
The influenza lifecycle heavily involves neuraminidase-mediated sialic acid cleavage. This enzyme contributes to pathways by enabling the efficient release of new viral particles enhancing the infectivity of the virus. Neuraminidase operates in concert with hemagglutinin which initially binds the virus to host cells by attaching to the sialic acid residues. This interplay is vital in viral replication pathways which propagate the infection cycle.
Specifications
Form
Liquid
Additional notes
ab131685 was purified using conventional chromatography techniques.
General info
Function
Catalyzes the removal of sialic acid (N-acetylneuraminic acid) moieties from glycoproteins and glycolipids. To be active, it is strictly dependent on its presence in the multienzyme complex. Appears to have a preference for alpha 2-3 and alpha 2-6 sialyl linkage.
Sequence similarities
Belongs to the glycosyl hydrolase 33 family.
Post-translational modifications
N-glycosylated.. Phosphorylation of tyrosine within the internalization signal results in inhibition of sialidase internalization and blockage on the plasma membrane.
Subcellular localisation
Lysosome membrane
Target data
Product promise
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