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11585886001

Roche

Neuraminidase (Sialidase)

from Clostridium perfringens

Sinônimo(s):

Sialidase

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About This Item

Número da licença da enzima:
Código UNSPSC:
12352204

fonte biológica

bacterial (Clostridium perfringens)

Nível de qualidade

Formulário

lyophilized

atividade específica

100 U/mg
~100 units/mg protein

peso molecular

60 kDa

embalagem

pkg of 5 U

fabricante/nome comercial

Roche

pH ideal

5

Condições de expedição

wet ice

temperatura de armazenamento

2-8°C

Descrição geral

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

Especificidade

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.

Aplicação

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

Ações bioquímicas/fisiológicas

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

Nota de preparo

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.

Outras notas

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

Código de classe de armazenamento

11 - Combustible Solids

Classe de risco de água (WGK)

WGK 1

Ponto de fulgor (°F)

does not flash

Ponto de fulgor (°C)

does not flash


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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
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)
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
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

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