产品描述信息
NR-19235?? N1 Neuraminidase (NA) Protein with N-Terminal Histidine Tag from Influenza Virus, A/Puerto Rico/8/1934 (H1N1), Recombinant from Baculovirus(Proteins)|Influenza A virus|N1 Neuraminidase (NA) Protein with N-Terminal Histidine Tag from Influenza Virus, A/Puerto Rico/8/1934 (H1N1), Recombinant from Baculovirus|2°C to 8°C|BEI ResourcesAcknowledgment for publications should read "The following reagent was obtained through BEI Resources, NIAID, NIH: N1 Neuraminidase (NA) Protein with N-Terminal Histidine Tag from Influenza Virus, A/Puerto Rico/8/1934 (H1N1), Recombinant from Baculovirus, NR-19235."|Quantity limit per order for this item is 1. This item can be ordered twice a year. Orders over this limit will be sent to NIAID for approval.
This item is currently in our production queue. Please allow ample time for distribution lots to be made available.
A recombinant form of the N1 neuraminidase (NA) protein from influenza A virus, A/Puerto Rico/8/1934 (H1N1) containing an N-terminal histidine tag was produced in High Five? insect cells using a baculovirus expression vector system and was purified by nickel affinity chromatography under denaturing conditions. The purified protein was refolded by dialysis and filtered.
NR-19235 was expressed from the same recombinant baculovirus vector as NR-42002, which was partially purified from culture supernatants under non-denaturing conditions and is enzymatically active.
The predicted ectodomain coding region of the NA gene was fused to a synthetic gene segment encoding an N-terminal eight-histidine tag followed by a 43 amino acid tetramerization domain from vasodilator-stimulated phosphoprotein (VASP) and a thrombin cleavage site.
Each vial contains approximately 50 to 150 ?g of purified recombinant NA protein in 50 mM Tris-HCl (pH 8.5), 240 mM NaCl, 10 mM KCl, 1 mM EDTA, 0.5 M Arginine, 0.5% Triton X-100, and 1 mM DTT.
NR-19235 has not been tested for enzymatic activity. Previous work at BEI Resources indicated that other influenza virus neuraminidases purified under denaturing conditions and refolded by dialysis are not able to cleave the fluorogenic substrate 2?-(4-methylumbelliferyl)-a-D-N-acetylneuraminic acid (4-MUNANA).