Product Details

Purity

>85% (SDS-PAGE)

Target Names

Uniprot No.

P03468

Alternative Names

NA; Neuraminidase; EC 3.2.1.18

Species

Influenza A virus (strain A/Puerto Rico/8/1934 H1N1)

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

we also demonstrate that NA[neuraminidase] mutations at residue Q136 can confer reduced zanamivir, peramivir or laninamivir susceptibility. PMID: 26608955
study found six mutations in NA genes of five independent dextran sulfate resistant viruses and each resistant NA gene had two mutations; all mutations were from basic to acidic or neutral amino acids PMID: 25234090
ACE2 cleavage is regulated by influenza A H1N1 neuraminidase. PMID: 24662240
NS genes can impact pathogenicity, histopathology, and cytokine production in mice. PMID: 24269912
Deletion of cysteine from the stalk region of NA in A/Ohio/07/2009 (H1N1) increases infectivity. PMID: 25118377
The T289M mutation eliminated the detrimental effect caused by the H275Y change in vitro while causing greater weight loss and mortality in mice. PMID: 24257597
Histidine-to-tyrosine substitution in the neuraminidase showed increased growth properties and virulence. PMID: 23924955
ETT was observed to detach from NA, on the contrary, both Zanamivir and our designed ligand bind NA firmly. PMID: 24015302
Multiple clusters of A(H1N1)pdm09 virus circulated in severe cases of influenza during the 2010-2011 season. PMID: 23588719
Data suggest that a conserved peptide region in the neuraminidase (NA)(denoted HCA-2) could either directly bind to the substrate or contribute to the formation of the active site in NA. PMID: 23645684
analysis of comparable fitness and transmissibility between oseltamivir-resistant pandemic 2009 and seasonal H1N1 influenza viruses with the H275Y neuraminidase mutation PMID: 22811535
Long time scale GPU dynamics reveal the mechanism of drug resistance of the dual mutant I223R/H275Y neuraminidase from H1N1-2009 influenza virus. PMID: 22574858
Neuraminidase modulates the of infectivity H1N1 influenza A virusin mice model. PMID: 22321413
Q222R reversion mutation in neuramindiase compromised Bris07-like H1N1 virus in vitro and in vivo. PMID: 22174688
Oseltamivir-resistance due to substitution of histidine by tyrosine at residue 275 (H275Y) of neuraminidase was not found in Malay patients indicating their viral isolates belong to the wild type and do not confer resistance to oseltamivir. PMID: 21323171
Amino acid substitution in neuroamonidase of pandemic (H1N1) 2009 virus may influence oseltamivir resistance of this virus. PMID: 21122225
the rapid emergence of the H275Y resistance mutation in individuals with severe A/H1N1 09 infection receiving neuraminidase inhibitors PMID: 20385168
Neuraminidase stability of enzymatic activity is unaffected by the SIINFEKL epitope during antigen processing in both murine L-Kb fibroblast cells and DC2.4 dendritic/monocyte cells. PMID: 20038640
These results confirm the potent inhibitory effect of A-315675 against oseltamivir-resistant influenza viruses of the N1 and N2 subtypes. PMID: 17919743
A structural model of the H1N1 neuraminidase. PMID: 18645233

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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:956530

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Recombinant Influenza A virus Neuraminidase (NA), partial

Product Details

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Target Background

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