Product Details

Purity

>85% (SDS-PAGE)

Target Names

Uniprot No.

Q9Q0U7

Alternative Names

NA; Neuraminidase; EC 3.2.1.18

Species

Influenza A virus (strain A/Goose/Guangdong/1/1996 H5N1 genotype Gs/Gd)

Protein Length

Partial

Tag Info

Tag type will be determined during the manufacturing process.

The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Form

Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer before Lyophilization

Tris/PBS-based buffer, 6% Trehalose, pH 8.0

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Lead Time

Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet

Please contact us to get it.

Target Background

Function

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.

Gene References into Functions

Neuraminidase of Influenza A virus binds lysosome-associated membrane proteins directly and induces lysosome rupture. PMID: 26246576
The results of the study reveal that amino acid residues 7-15 of H5N1 NA are critical for its biosynthetic transport to the host cell surface. PMID: 25458889
Influenza A Virus, H5N1 Subtype with a R292K NA mutation are highly resistant to the oseltamivir. PMID: 23794010
Cysteine deletion in the stalk region is important for the infectivity of A/Anhui/1/05 (H5N1). PMID: 25118377
Loss of the neuraminidase protein and enzymatic activity did not affect virus replication efficiency. PMID: 24109212
Data indicate that recombinant viruses, rPR8-H1N1NA, rPR8-H5N1NA, and rPR8-H9N2NA, were shown to have similar growth kinetics in cells and pathogenicity in mice, but witih differential effects on virus release, and cell-cell fusion. PMID: 23349854
The evolutionary pattern of glycosylation sites in influenza virus (H5N1) hemagglutinin and neuraminidase PMID: 23133677
highly pathogenic H5N1 variants carrying mutations within the NA active site that decrease susceptibility to NA inhibitors may possess increased virulence in mammalian hosts compared to drug-sensitive viruses PMID: 20523902
Results describe the individual contributions of each of the three HPAIV surface proteins -- hemagglutinin (HA), neuraminidase (NA), and M2 -- to the induction of HPAIV-neutralizing serum antibodies and protective immunity in chickens. PMID: 20032181
15 or 20 amino acids deletion in NA stalk had a pronounced effect on virus growth ability in MDCK cells PMID: 17037051
short-stalk NA of H5N1 viruses circulating in Asia may contribute to virulence in humans PMID: 19225004

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Subcellular Location

Virion membrane. Host apical cell membrane; Single-pass type II membrane protein.

Protein Families

Glycosyl hydrolase 34 family

Database Links

KEGG: vg:3654619

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Recombinant Influenza A virus Neuraminidase (NA), partial

Product Details

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Target Background

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