- SynonymNA,Neuraminidase
- SourceInfluenza A [A/Thailand/1(KAN-1)/2004 (H5N1)] NA, His Tag (H54-V5247) is expressed from human 293 cells (HEK293). It contains AA His 36 - Lys 449 (Accession # H8PF47).Predicted N-terminus: HisRequest for sequence
- Molecular Characterization
This protein carries a polyhistidine tag at the N-terminus.
The protein has a calculated MW of 46.1 kDa. The protein migrates as 50-57 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.
- EndotoxinLess than 1.0 EU per μg by the LAL method.
- Purity
>92% as determined by SDS-PAGE.
- Formulation
Lyophilized from 0.22 μm filtered solution in PBS, pH7.4. Normally trehalose is added as protectant before lyophilization.
Contact us for customized product form or formulation.
- Reconstitution
Please see Certificate of Analysis for specific instructions.
For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
- Storage
For long term storage, the product should be stored at lyophilized state at -20°C or lower.
Please avoid repeated freeze-thaw cycles.
This product is stable after storage at:
- -20°C to -70°C for 12 months in lyophilized state;
- -70°C for 3 months under sterile conditions after reconstitution.
Influenza A [A/Thailand/1(KAN-1)/2004 (H5N1)] NA, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 92%.
- BackgroundNeuraminidase (NA) and hemagglutinin (HA) are major membrane glycoproteins found on the surface of influenza virus. Hemagglutinin binds to the sialic acid-containing receptors on the surface of host cells during initial infection and at the end of an infectious cycle. Neuraminidase, on the other hand, cleaves the HA-sialic acid bondage from the newly formed virions and the host cell receptors during budding. Neuraminidase thus is described as a receptor-destroying enzyme which facilitates virus release and efficient spread of the progeny virus from cell to cell.
- References
- (1)Manz B., et al., 2012, Submitted to the EMBL/GenBank/DDBJ databases.
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