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N5254

Sigma-Aldrich

Neuraminidase Agarose from Clostridium perfringens (C. welchii)

Type VI-A, ammonium sulfate suspension

Sinonimo/i:

Acylneuraminyl hydrolase, Receptor-destroying enzyme, Sialidase

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About This Item

Classificazione EC (Enzyme Commission):
3.2.1.18 (BRENDA, IUBMB)
Numero MDL:
MFCD00131711
Codice UNSPSC:
12352204
NACRES:
NA.54

Tipo

Type VI-A

Forma fisica

ammonium sulfate suspension

Attività specifica

20-60 units/g agarose

Grado di funzionalizzazione

0.6-1.8 units per mL gel
20-60 units per g agarose

Matrice

beaded agarose

Temperatura di conservazione

2-8°C

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Descrizione generale

Neuraminidase enzymes are glycoside hydrolase enzymes that catalyze hydrolysis of terminal sialic acid residues. The most well-known are the viral nearamidases, which promote influenza virus release.

Applicazioni

Agarose-linked neuraminidase from Clostridium perfringens can be used for the detection of total and desialylated sex hormone-binding globulin in human serum samples.
Neuraminidase from Clostridium perfringens has been used in a study to assess a genetic polymorphism of human serum glycoprotein (inter-α-trypsin-inhibitor). It has also been used in a study to investigate the inhibition of neuraminidase by chemically sulphated glycopeptides.

Definizione di unità

One unit will liberate 1.0 μmole of N-acetylneuraminic acid per min at pH 5.0 at 37 °C using NAN-lactose or bovine submaxillary mucin, unless otherwise specified. Prices based on units using NAN-lactose as substrate.

Stato fisico

Suspension in 2.0 M (NH4)2SO4 solution, pH 7.0.

Nota sulla preparazione

Prepared from Neuraminidase, Type VI (N 3001).

Codice della classe di stoccaggio

12 - Non Combustible Liquids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Certificati d'analisi (COA)

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The mechanisms controlling the recognition of tumor- and virus-infected cells by NKp46
Arnon, T.I., et al
Immunobiol., 103(2), 664-672 (2004)
N Mian et al.
The Biochemical journal, 181(2), 377-385 (1979-08-01)
Chemically sulphated glycopeptides (derived from pig duodenal mucosa) inhibited Clostridium perfringens neuraminidase (EC 3.2.1.18) activity in a pH-dependent manner. Analysis of inhibition kinetics data indicated that, although the enzyme inhibition could not be categorized into any of the classical types
T I Arnon et al.
European journal of immunology, 31(9), 2680-2689 (2001-09-06)
Natural killer (NK) cells destroy virus-infected and tumor cells without prior antigen stimulation. The NK cell cytotoxicity is regulated in large part by the expression of NK cell receptors that are able to bind major histocompatibility complex (MHC) class I
Measurements of total and desialylated sex hormone binding globulin in serum by ELISA.
J Vaysse et al.
Clinical chemistry, 44(4), 882-884 (1998-04-29)
U Vogt et al.
Human genetics, 84(2), 151-154 (1990-01-01)
A new genetic polymorphism of a human serum glycoprotein, the inter-alpha-trypsin-inhibitor (ITI), has been demonstrated by population and family studies. Sera were examined after neuraminidase treatment by isoelectric focusing on agarose gels followed by immunoblotting or by immunofixation with specific
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