11585886001
Roche
Neuraminidase (Sialidase)
from Clostridium perfringens
Synonyme(s) :
Sialidase
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About This Item
Produits recommandés
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:
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.
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
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Les clients ont également consulté
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
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
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)
Role of neuraminidase in influenza virus-induced apoptosis.
Morris S J, et al.
The Journal of General Virology, 80(1), 137-146 (1999)
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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