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N7885

Sigma-Aldrich

Neuraminidase from Vibrio cholerae

Type III, buffered aqueous solution, 0.2 μm filtered, 1-5 units/mg protein (Lowry, using NAN-lactose)

Sinónimos:

Acyl-neuraminyl Hydrolase, Receptor-destroying enzyme, Sialidase

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About This Item

Número de CAS:
9001-67-6
Comisión internacional de enzimas:
3.2.1.18 (BRENDA, IUBMB)
EC Number:
232-624-6
MDL number:
MFCD00131711
UNSPSC Code:
12352204
NACRES:
NA.54

Quality Level

300

type

Type III

form

buffered aqueous solution

specific activity

1-5 units/mg protein (Lowry, using NAN-lactose)

mol wt

83 kDa

application(s)

diagnostic assay manufacturing

foreign activity

Protease and NAN-aldolase, present

storage temp.

2-8°C

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General description

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.

Application

Neuraminidase from Vibrio cholerae has been used in a study to assess its role in the binding and uptake of cholera toxin by susceptible cells. It has also been used in a study to investigate the preparation of a sodium substrate and its use in a fluorometric assay of neuraminidase.
Neurminidase is used as a cell-surface probe for glycoconjugate distribution and in substrate specificity studies.

Biochem/physiol Actions

Vibrio cholerae neuraminidase has been shown to promote cholera toxin infection by binding the toxin and aiding in its uptake by cells.

Quality

Preservative free.

Unit Definition

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.

Physical form

Aqueous solution, pH 5.5, containing 0.15 M NaCl and 4 mM CaCl2.

Preparation Note

Chromatographically purified.

substrate

Referencia del producto
Descripción
Precios

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

Storage Class

10 - Combustible liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Jai Woong Seo et al.
Nature communications, 11(1), 2102-2102 (2020-05-02)
Adeno-associated viruses (AAVs) are typically single-stranded deoxyribonucleic acid (ssDNA) encapsulated within 25-nm protein capsids. Recently, tissue-specific AAV capsids (e.g. PHP.eB) have been shown to enhance brain delivery in rodents via the LY6A receptor on brain endothelial cells. Here, we create
J E Galen et al.
Infection and immunity, 60(2), 406-415 (1992-02-01)
Vibrio cholerae neuraminidase (NANase) is hypothesized to act synergistically with cholera toxin (CT) and increase the severity of a secretory response by increasing the binding and penetration of CT to enterocytes. To test this hypothesis, the NANase gene (nanH) from
Fluorometric assay of neuraminidase with a sodium (4-methylumbelliferyl-alpha-D-N-acetylneuraminate) substrate.
M Potier et al.
Analytical biochemistry, 94(2), 287-296 (1979-04-15)
Mikhail N Matrosovich et al.
Methods in molecular biology (Clifton, N.J.), 865, 71-94 (2012-04-25)
Influenza virus attachment to sialic acid-containing molecules on the cell surface initiates the infection. The spectrum of functional receptors on target cells and decoy receptors on cells and epithelial mucus varies substantially between animal species leading to variations in the
Lenka Horníková et al.
Current protocols in microbiology, 38, 14F-14F (2015-08-04)
Mouse polyomavirus (MPyV) is a member of the Polyomaviridae family, which comprises non-enveloped tumorigenic viruses infecting various vertebrates including humans and causing different pathogenic responses in the infected organisms. Despite the variations in host tropism and pathogenicity, the structure of
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