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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

Synonyme(s) :

Acyl-Neuraminyl Hydrolase, Sialidase

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About This Item

Numéro de classification (Commission des enzymes):
3.2.1.18 (BRENDA, IUBMB)
Numéro MDL:
MFCD01092201
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.32

Produit recombinant

expressed in E. coli

Niveau de qualité

200

Forme

buffered aqueous solution

Activité spécifique

≥250 units/mg protein

Poids mol.

~41 kDa

Activité étrangère

proteases, none detected

Conditions d'expédition

wet ice

Température de stockage

2-8°C

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Actions biochimiques/physiologiques

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

Conditionnement

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

Définition de l'unité

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

Forme physique

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

Notes préparatoires

Expressed in glycosidase-free hosts.

Pictogrammes

Health hazard
GHS08

Mention d'avertissement

Danger

Mentions de danger

H334

Conseils de prudence

P261 - P284 - P501

Classification des risques

Resp. Sens. 1

Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)

Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

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
Andreas Max Ernst et al.
FEBS letters, 587(9), 1411-1417 (2013-03-26)
Influenza A Neuraminidase is essential for virus release from the cell surface of host cells. Given differential structures of the N-terminal sequences including the transmembrane domains of neuraminidase subtypes, we investigated their contribution to transport and localization of subtypes N1
Ramaiah Arunachalam et al.
Interdisciplinary sciences, computational life sciences, 4(4), 282-290 (2013-01-29)
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
E V Kostina et al.
Bioorganicheskaia khimiia, 38(6), 676-682 (2013-04-04)
The microchip for influenza A subtyping was developed, functioning on a principle "one spot--one subtype". Each spot contains the set of oligonucleotide probes, specific for a particular subtype of hemagglutinin, neuraminidase or matrix gene. Reliability of the proposed chip version
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