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11080725001

Roche

Neuraminidase (Sialidase)

from Vibrio cholerae

Synonym(s):

Salidase

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About This Item

Enzyme Commission number:
UNSPSC Code:
12352204

biological source

Vibrio cholerae

Quality Level

form

solution

mol wt

~95 kDa

packaging

pkg of 1 U

manufacturer/tradename

Roche

optimum pH

5.5-6.2

suitability

suitable for ELISA applications

application(s)

life science and biopharma
sample preparation

shipped in

wet ice

storage temp.

2-8°C

Related Categories

General description

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.).

Specificity

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

Unit Definition

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.

Physical form

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.

Other Notes

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

Legal Information

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.

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Hazard Classifications

Skin Sens. 1

wgk_germany

WGK 1

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flash_point_c

does not flash


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
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
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
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)

Protocols

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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