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Merck

N5521

Sigma-Aldrich

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

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

Synonym(e):

Sialidase

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About This Item

EC-Nummer:
MDL-Nummer:
UNSPSC-Code:
12352204
NACRES:
NA.32

Rekombinant

expressed in E. coli

Qualitätsniveau

Form

buffered aqueous solution

Spezifische Aktivität

≥250 units/mg protein

Mol-Gew.

~41 kDa

Fremdaktivität

proteases, none detected

Versandbedingung

wet ice

Lagertemp.

2-8°C

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Biochem./physiol. Wirkung

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

Verpackung

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

Einheitendefinition

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

Physikalische Form

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

Angaben zur Herstellung

Expressed in glycosidase-free hosts.

Piktogramme

Health hazard

Signalwort

Danger

H-Sätze

Gefahreneinstufungen

Resp. Sens. 1

Lagerklassenschlüssel

12 - Non Combustible Liquids

WGK

WGK 1

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Gloves, type N95 (US)


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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
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
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
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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