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11585886001
Roche
Neuraminidase (Sialidase)
from Clostridium perfringens
Synonim(y):
Sialidase
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About This Item
Polecane produkty
pochodzenie biologiczne
bacterial (Clostridium perfringens)
Poziom jakości
Postać
lyophilized
aktywność właściwa
100 U/mg
~100 units/mg protein
masa cząsteczkowa
60 kDa
opakowanie
pkg of 5 U
producent / nazwa handlowa
Roche
optymalne pH
5
Warunki transportu
wet ice
temp. przechowywania
2-8°C
Opis ogólny
approximately 100 U/mg protein at +37°C and pH 5.0 with N-acetyl-neuraminosyl-D-lactose as the substrate.
Specyficzność
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.
Zastosowanie
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
Działania biochem./fizjol.
Neuraminidase breaks α-ketosidic linkage between N-acetylneuraminic acid and the adjacent sugar residue.
Neuraminidase mediates apoptosis in the host cell before viral entry.
Uwaga dotycząca przygotowania
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.
Inne uwagi
For life science research only. Not for use in diagnostic procedures.
This page may contain text that has been machine translated.
Kod klasy składowania
11 - Combustible Solids
Klasa zagrożenia wodnego (WGK)
WGK 1
Temperatura zapłonu (°F)
does not flash
Temperatura zapłonu (°C)
does not flash
Certyfikaty analizy (CoA)
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