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11585886001

Roche

Neuraminidase (Sialidase)

from Clostridium perfringens

Synonym(s):

Sialidase

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5 UNITS
$222.00

$222.00


Available to ship onApril 29, 2025Details



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5 UNITS
$222.00

About This Item

Enzyme Commission number:
UNSPSC Code:
12352204

$222.00


Available to ship onApril 29, 2025Details


biological source

bacterial (Clostridium perfringens)

Quality Level

form

lyophilized

specific activity

100 U/mg
~100 units/mg protein

mol wt

60 kDa

packaging

pkg of 5 U

manufacturer/tradename

Roche

optimum pH

5

shipped in

wet ice

storage temp.

2-8°C

General description

approximately 100 U/mg protein at +37°C and pH 5.0 with N-acetyl-neuraminosyl-D-lactose as the substrate.

Specificity

Cleaves terminal sialic-acid residues that are α2,3-, α2,6-, or α2,8-linked to Gal, GlcNAc, GalNAc, AcNeu, GlcNeu, oligosaccharides, glycolipids, or glycoproteins. Relative rate of cleavage is α2,3 >α2,8 = α2,6, determined on bonds in tri- and tetrasaccharides.

Application

Neuraminidase (Sialidase) has been used to desialylate transferrin in order to study its isoforms in human serum.[1]
Use Neuraminidase to hydrolyze terminal N- or 0-acylneuraminic acids which are α2,3-, α2,6-, or α2,8-linked (rate α2,3: > α2,6 = α2,8) to oligosaccharides, polysaccharides, mucopolysaccharides, glycoproteins, and glycolipids.In contrast to the enzyme from Arthrobacter ureafaciens, neuraminidase from Clostridium perfringens hydrolyzes α2,3-linkages faster than α2,6-linkages. α2,8-bound sialic acids area cleaved with a similar velocity compared to α2,6-bound sialic acids.
Neuraminidase is used for:
  • Virus receptor studies
  • Studies on the interaction of lymphocytes with tumor cells
  • Cell hybridizations
  • Analysis of oligosaccharides
  • Analysis of glycoproteins[1][2]
  • Analysis of glycolipids

Biochem/physiol Actions

Neuraminidase breaks α-ketosidic linkage between N-acetylneuraminic acid and the adjacent sugar residue.[3]
Neuraminidase mediates apoptosis in the host cell before viral entry.[4]

Preparation Note

Stabilizers: The enzyme can be stabilized by bovine serum albumin (BSA).
Storage conditions (working solution): After reconstitution in double-dist. water or sample buffer, the enzyme is stable for several weeks, stored at 2 to 8 °C; for longer storage, freezing is recommended. A stock solution may be made (e.g., at c = 5 U/100 μl). The enzyme looses approx. 50% of its activity after incubation at 37 °C for 24 hours.

Other Notes

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

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

does not flash

flash_point_c

does not flash


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Analysis of genetic variants of transferrin in human serum after desialylation by capillary zone electrophoresis and capillary isoelectric focusing
Caslavska J, et al.
Journal of Separation Science, 40(11), 2488-2497 (2017)
Fast, robust and high-resolution glycosylation profiling of intact monoclonal IgG antibodies using nanoLC-chip-QTOF
Jacobs JF, et al.
Clinica Chimica Acta; International Journal of Clinical Chemistry, 461, 90-97 (2016)
Mito Kanatsu-Shinohara et al.
Cell reports. Medicine, 3(5), 100606-100606 (2022-05-19)
Oocytes and granulosa cells closely interact with each other during follicular development, and a lack of appropriate signaling between them results in infertility. Attempts to manipulate oocyte microenvironment have been impeded by the impermeability of the blood-follicle barrier (BFB). To
Jitka Caslavska et al.
Journal of separation science, 40(11), 2488-2497 (2017-04-04)
Capillary electrophoresis analysis of transferrin in human serum is used to assess genetic variants after desialylation with neuraminidase and iron saturation to reduce the complexity of the transferrin pattern and thus facilitate the recognition of transferrin polymorphisms. Asialo-transferrin forms are
Ryan Septa Kurnia et al.
Veterinary world, 15(8), 1896-1905 (2022-11-01)
Clostridium toxins are widely used as medicinal agents. Many active metabolic enzymes, including sialidase (neuraminidase), hyaluronidase, and collagenase, contribute to the mechanism of action of these toxins. Sialidase from Clostridium perfringens recognizes and degrades sialic acid receptors in the host

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