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11585886001

Roche

Neuraminidase (Sialidase)

from Clostridium perfringens

Synonyme(s) :

Sialidase

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About This Item

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

Source biologique

bacterial (Clostridium perfringens)

Niveau de qualité

Forme

lyophilized

Activité spécifique

100 U/mg
~100 units/mg protein

Poids mol.

60 kDa

Conditionnement

pkg of 5 U

Fabricant/nom de marque

Roche

pH optimal

5

Conditions d'expédition

wet ice

Température de stockage

2-8°C

Description générale

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

Spécificité

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.
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
  • Analysis of glycolipids

Actions biochimiques/physiologiques

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

Notes préparatoires

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.

Autres remarques

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

Code de la classe de stockage

11 - Combustible Solids

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)

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Consulter la Bibliothèque de documents

Role of neuraminidase in influenza virus-induced apoptosis.
Morris S J, et al.
The Journal of General Virology, 80(1), 137-146 (1999)
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
Jesús S Aguilar Díaz de León et al.
Journal of Cancer, 12(16), 4993-5004 (2021-07-09)
Elevated concentrations of circulating low density lipoprotein (LDL) that is abnormally oxidized and desialylated is both a precursor to and a hallmark of atherosclerosis. Peripheral blood mononuclear cells (PBMCs) treated in vitro with interleukin-2 (IL-2) become lymphokine activated killer (LAK)
Y A Shtyrya et al.
Acta naturae, 1(2), 26-32 (2009-07-01)
The structure of the influenza virus neuraminidases, the spatial organization of their active site, the mechanism of carbohydrate chains desialylation by neuraminidase, and its role in the influenza virus function at different stages of the viral infectious cycle are considered

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