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11080725001

Roche

Neuraminidase (Sialidase)

from Vibrio cholerae

Synonyme(s) :

Salidase

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About This Item

Numéro de classification (Commission des enzymes):
Code UNSPSC :
12352204

Source biologique

Vibrio cholerae

Niveau de qualité

Forme

solution

Poids mol.

~95 kDa

Conditionnement

pkg of 1 U

Fabricant/nom de marque

Roche

pH optimal

5.5-6.2

Adéquation

suitable for ELISA applications

Application(s)

life science and biopharma
sample preparation

Conditions d'expédition

wet ice

Température de stockage

2-8°C

Description générale

Approximately 40 U/mg enzyme protein at 37 °C and pH 5.5, with N-acetyl-neuraminosyl-D-lactose as the substrate.
Neuraminidase is an acylneuraminyl hydrolase which hydrolyzes terminal N- or O-acylneuraminic acids which are α2,3-, α2,6-, or α2,8-linked (rate: α2,6 > α2,3 > α2,8) to oligosaccharides, polysaccharides, mucopolysaccharides, glycoproteins, and glycolipids. Noteworthy, for the hydrolysis of glycolipids, the presence of a detergent is necessary. Because of the broad substrate specificity, the enzyme is very well suited for the complete removal of sialic acids from glycoconjugates of a wide variety of biological materials (e.g., in cytology, on cell surfaces, viruses etc.).

Spécificité

Hydrolyzes terminal N- or O-acyl-neuraminic acids that are α2,3-, α2,6-, or α2,8-linked to galactose, Hex, NAc, or N- or O-acylated neuraminyl residues in oligosaccharides/glycoconjugates or colominic acid. Relative rate of cleavage is α2,3 >α2,6 >α2,8, determined on bonds in tri- and tetrasaccharides.

Application

Neuraminidase has been used:
  • to remove cis-acting sialic acids in CHO (chinese hamster ovary) cells
  • for deglycosylation studies

Définition de l'unité

One unit is the enzyme activity that hydrolyzes 1 μmol N-acetyl-neuraminosyl-D-lactose within 1 min at +37 °C under the following incubation conditions:
10 mM N-acetyl-neuraminosyl-D-lactose, 50 mM sodium acetate, 4 mM calcium chloride, bovine serum albumin, 100 μg/ml, pH 5.5. The activity is determined by measuring the released D-lactose using the β-galactosidase/galactose dehydrogenase method. Under the same conditions, 1 μmol N-acetylneuraminic acid per min is split off from human acid α1-glycoprotein (10 mg/ml incubation mixture) by 1 U neuraminidase. Released N-acetyl-neuraminic acid can be determined using, for example, the thiobarbituric acid method.

Forme physique

Solution in 50 mM sodium acetate, 154 mM sodium chloride, 9 mM calcium chloride, 0.1% Micr-O-Protect (w/v), human serum albumin, 25 mg/l, pH 5.5. The preparation contains 10 mM EDTA.
Note: The serum used for this preparation was tested for HBs antigen and for the presence of antibodies to HIV-1, HIV-2, HCV, and found to be negative, according to the current quality control procedures.

Autres remarques

For life science research only. Not for use in diagnostic procedures.

Informations légales

The sale of the Product does not exhaust or grant any rights in third party patents including patents of companies of the F. Hoffmann - La Roche AG group of companies, in particular, for the use of modified antibodies obtained by using the product.

Pictogrammes

Exclamation mark

Mention d'avertissement

Warning

Mentions de danger

Classification des risques

Skin 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)

does not flash

Point d'éclair (°C)

does not flash


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

Direct Attachment with Erythrocytes Augments Extracellular Growth of Pathogenic Mycobacteria.
Nishiuchi, et al.
Microbiology spectrum, 10, e0245421-e0245421 (2022)
Angeles Canales et al.
JACS Au, 3(3), 868-878 (2023-04-04)
Influenza virus infection remains a threat to human health since viral hemagglutinins are constantly drifting, escaping infection and vaccine-induced antibody responses. Viral hemagglutinins from different viruses display variability in glycan recognition. In this context, recent H3N2 viruses have specificity for
Misako Nakayama et al.
Methods in molecular biology (Clifton, N.J.), 2556, 37-43 (2022-09-30)
Hemagglutinin (HA) on the surface of influenza viruses binds to sialic acids, mainly N-acetylneuraminic acid (Neu5Ac) or N-glycolylneuraminic acid. Neu5Ac and N-glycolylneuraminic acid lie at the terminal end of sugar chains on the cell surface. Human influenza viruses preferentially bind
Peter L Delputte et al.
Journal of virology, 81(17), 9546-9550 (2007-06-15)
The sialic acid-binding lectin sialoadhesin (Sn) is a macrophage-restricted receptor for porcine reproductive and respiratory syndrome virus (PRRSV). To investigate the importance of pSn sialic acid-binding activity for PRRSV infection, an R(116)-to-E mutation was introduced in the predicted sialic acid-binding
A previously uncharacterized O-glycopeptidase from Akkermansia muciniphila requires the Tn-antigen for cleavage of the peptide bond.
Medley, et al.
The Journal of biological chemistry, 298, 102439-102439 (2023)

Protocoles

Neuraminidase can be used to cleave sialic acids from proteins. In this protocol, the enzyme from Vibrio cholerae is used on fixed cells.

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