Neuraminidase des perfrinogènes de Clostridium (c.?áwelchii), Type VIII, poudre lyophilisée, 10-20 unités/mg de protéines (à l'aide de4˚- NANA), 3,5-8,0 unités/mg de protéines (mucine)

Code: n5631-10un D2-231

Non disponible en dehors du Royaume-Uni et de l'Irlande

Analysis Note

Package sizes based on 4MU-NANA units

Package sizes based on the 4MU-NANA units

Application

Neuraminidase from Clostridiu...


en savoir plus

Votre prix
£828.00 EACH

Non disponible en dehors du Royaume-Uni et de l'Irlande

Analysis Note

Package sizes based on 4MU-NANA units

Package sizes based on the 4MU-NANA units

Application

Neuraminidase from Clostridium perfringens has been used in a study to assess the binding characteristics of iota toxin by fluorescence-activated cytometry. It has also been used in a study to investigate the distribution of neuraminidase among food poisoning strains.

Biochem/physiol Actions

The degradation of gangliosides grown in lipid mono layers by Clostridium perfringens neuraminidase depends largely on surface pressure. Increased pressure can inhibit neuraminidase activity.

Neuraminidases are used to cleave terminal N-acetyl neuraminic acid (sialic acid) from a variety of glycoproteins. The enzyme from Clostridium perfringens cleaves terminal sialic acid residues which are α-2,3- α-2,6- or α-2,8-linked to Gal, GlcNac, GalNAc, AcNeu, GlcNeu, oligosaccharides, glycolipids or glycoproteins. The relative rate of cleavage decreases in the order: α-2-3 > α-2-6 . α-2-8. Neuraminidase from C. perfringens cleaves α-2-3 linked sialic acid residues most efficiently, compared to A. ureafaciens, (Sigma N3642) which preferentially cleaves α-2-6 linked residues.

The use of neuraminidase to remove sialic acid residues from glycoproteins on cell surfaces has been frequently reported. Generally, procedures have indicated using neuraminidase in PBS at 37°C for 30 minutes, followed by several washings with PBS. Treatment of tissue sections with neuraminidase at much lower concentrations require longer incubation: for 1-4 U/mL in 0.1 M acetate buffer pH 4.2-5, from 2 to 20 hours at 37 °C.

Neuraminidase cleavage of sialic acid groups has been used to study recognition by antibodies of glycoprotein structures. The use of neuraminidase in the estimation of N-acetylneuraminic acid was compared favorably to two other methods.

General description

Neuraminidase enzymes are glycoside hydrolase enzymes that catalyze hydrolysis of terminal sialic acid residues. The most well-known are the viral nearamidases, which promote influenza virus release.

Preparation Note

Chromatographically purified from Type V (N 2876)

Unit Definition

One unit will liberate 1.0 micromole of N-acetyl neuraminic acid per minute at pH 5.0 at 37 °C using bovine submaxillary mucin.One unit will hydrolyze 1.0 micromole of 2′-(4-methylumbelliferyl)-a-D-N-actetylneuraminic acid per minute at pH 5.0 at 37 °C (using 4MU-NANA as a substrate)

compositionProtein, ≥85% biuret
foreign activityProtease and NAN-aldolase, present
formlyophilized powder
Gene InformationClostridium perfringens str. 13 ... nanI(988807)
Quality Level200
specific activity10-20 units/mg protein (using 4MU-NANA), 3.5-8.0 units/mg protein (mucin)
storage temp.−20°C
typeType VIII
Cas Number9001-67-6
Ce produit répond aux critères suivants: