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Merck
CN

N5521

α(2→3,6) Neuraminidase from Clostridium perfringens (C. welchii)

recombinant, expressed in E. coli, buffered aqueous solution, ≥250 units/mg protein

别名:

唾液酸酶

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关于此项目

MDL编号:
UNSPSC代码:
12352204
NACRES:
NA.32
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重组

expressed in E. coli

质量水平

表单

buffered aqueous solution

比活

≥250 units/mg protein

分子量

~41 kDa

异质活性

proteases, none detected

运输

wet ice

储存温度

2-8°C

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生化/生理作用

Releases α(2→3)- and α(2→6)-linked N-acetylneuraminic acid from complex oligosaccharides.

包装

Provided with 5× reaction buffer (250 mM sodium phosphate, pH 6.0).

外形

Solution in 20 mM Tris-HCl, pH 7.5, and 25 mM NaCl.

制备说明

Expressed in glycosidase-free hosts.

其他说明

One unit will hydrolyze 1 μmole of 4-methylumbelliferyl α-D-N-acetylneuraminide per min at pH 5.0 at 37 °C

象形图

Health hazard

警示用语:

Danger

危险声明

预防措施声明

危险分类

Resp. Sens. 1

储存分类代码

12 - Non Combustible Liquids

WGK

WGK 1

闪点(°F)

Not applicable

闪点(°C)

Not applicable

个人防护装备

Eyeshields, Gloves, type N95 (US)

法规信息

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分析证书(COA)

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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
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
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
Longping V Tse et al.
Journal of virology, 87(9), 5161-5169 (2013-03-02)
Influenza virus is well recognized to modulate host tropism and pathogenesis based on mutations in the proteolytic cleavage site of the viral hemagglutinin (HA), which activates HA and exposes the fusion peptide for membrane fusion. Instead of the conventional trypsin-mediated

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