产品名称
α(2→3,6) Neuraminidase from Clostridium perfringens (C. welchii), recombinant, expressed in E. coli, buffered aqueous solution, ≥250 units/mg protein
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
Quality Level
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Biochem/physiol Actions
Releases α(2→3)- and α(2→6)-linked N-acetylneuraminic acid from complex oligosaccharides.
Other Notes
One unit will hydrolyze 1 μmole of 4-methylumbelliferyl α-D-N-acetylneuraminide per min at pH 5.0 at 37 °C
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.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
存储类别
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
法规信息
新产品
此项目有
Charles R Beck et al.
Influenza and other respiratory viruses, 7 Suppl 1, 14-24 (2013-02-12)
The objectives of this study were to: (1) reflect on key stages in the discovery, development and pre-pandemic use of neuraminidase inhibitors (NAIs), (2) summarise the evidence of NAI effectiveness for treatment and prophylaxis of seasonal influenza prior to the
Rodolfo Ocadiz-Delgado et al.
BMC infectious diseases, 13, 20-20 (2013-01-19)
In April 2009, public health surveillance detected an increased number of influenza-like illnesses in Mexico City's hospitals. The etiological agent was subsequently determined to be a spread of a worldwide novel influenza A (H1N1) triple reassortant. The purpose of the
Weijia Wang et al.
Journal of virology, 87(8), 4642-4649 (2013-02-15)
In 2009, we successfully produced a high-yield live attenuated H1N1pdm A/California/7/2009 vaccine (CA/09 LAIV) by substitution of three residues (K119E, A186D, and D222G) in the hemagglutinin (HA) protein. Since then, we have generated and evaluated additional H1N1pdm vaccine candidates from
S Bhatt et al.
Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 368(1614), 20120382-20120382 (2013-02-06)
Few questions on infectious disease are more important than understanding how and why avian influenza A viruses successfully emerge in mammalian populations, yet little is known about the rate and nature of the virus' genetic adaptation in new hosts. Here
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
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Understand sialic acid structure, function, signaling, and modifications. Easily find products for sialic acid research.
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