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A propos de cet article
Specific activity:
≥250 units/mg protein
Recombinant:
expressed in E. coli
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Laissez-nous vous aiderQuality Level
recombinant
expressed in E. coli
form
buffered aqueous solution
specific activity
≥250 units/mg protein
mol wt
~41 kDa
foreign activity
proteases, none detected
shipped in
wet ice
storage temp.
2-8°C
Catégories apparentées
Biochem/physiol Actions
Releases α(2→3)- and α(2→6)-linked N-acetylneuraminic acid from complex oligosaccharides.
Packaging
Provided with 5× reaction buffer (250 mM sodium phosphate, pH 6.0).
Physical form
Solution in 20 mM Tris-HCl, pH 7.5, and 25 mM NaCl.
Preparation Note
Expressed in glycosidase-free hosts.
Other Notes
One unit will hydrolyze 1 μmole of 4-methylumbelliferyl α-D-N-acetylneuraminide per min at pH 5.0 at 37 °C
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Classe de stockage
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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The aim of the present investigation was to discover the genetic relationships of 2009 pandemic novel influenza A/H1N1 virus (NIV) external antigens Hemagglutinin (HA) and Neuraminidase (NA) with other influenza viruses by performing phylogenetic, comparative and statistical analyses. Phylogenetic trees
Andrew T Pavia
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Respiratory viruses have long been appreciated as a cause of community acquired pneumonia (CAP), particularly among children, people with serious medical comorbidities, and military recruits. They are increasingly recognized as a cause of CAP among adults. Polymerase chain reaction-based testing
Quanjiao Chen et al.
PloS one, 8(1), e54334-e54334 (2013-01-26)
Two surface glycoproteins of influenza virus, haemagglutinin (HA) and neuraminidase (NA), play opposite roles in terms of their interaction with host sialic acid receptors. HA attaches to sialic acid on host cell surface receptors to initiate virus infection while NA
Johan Nordholm et al.
The Journal of biological chemistry, 288(15), 10652-10660 (2013-03-01)
Interactions that facilitate transmembrane domain (TMD) dimerization have been identified mainly using synthetic TMDs. Here, we investigated how inherent properties within natural TMDs modulate their interaction strength by exploiting the sequence variation in the nine neuraminidase subtypes (N1-N9) and the
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