Select a Size
All Photos(3)
About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-624-6
MDL number:
Product Name
Neuraminidase from Clostridium perfringens (C. welchii), Type X, lyophilized powder, ≥50 units/mg protein (using 4MU-NANA)
type
Type X
form
lyophilized powder
specific activity
≥50 units/mg protein (using 4MU-NANA)
storage temp.
−20°C
Quality Level
Gene Information
Clostridium perfringens str. 13 ... nanI(988807)
Looking for similar products? Visit Product Comparison Guide
Related Categories
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 purification via affinity chromatography. It has also been used in a study to investigate site-directed mutations of amino acids of the neuraminidase gene, nanH.
Biochem/physiol Actions
Neuraminidase can block attachment of type 3 reovirus to cell membranes. This effect is related to the ability of neuraminidase to hydrolysis sialic acid residues within cell surface receptors.
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.
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.
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.
Other Notes
One unit will hydrolyze 1.0 micromole of 2′-(4-Methylumbelliferyl)-alpha-D-N-actetylneuraminic acid per min at pH 5.0 at 37 °C.
Preparation Note
Purified by affinity chromatography from Type VIII (N 5631)
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Marjorie E Kanof
Current protocols in immunology, Chapter 7, 7-7 (2008-04-25)
This unit describes a procedure for separating T cells from other mononuclear cells by exploiting the unique ability of cells to bind to and form rosettes with sheep red blood cells (SRBC). This isolation method also allows recovery of the
C H Chien et al.
Enzyme and microbial technology, 19(4), 267-276 (1996-09-01)
The small nanH gene encoding the neuraminidase from Clostridium perfringens ATCC 10543 was cloned in JM109 using pUC19 as a vector. Sequence analysis revealed an ORF encoding 382 amino acids without a signal peptide sequence. Four regions of amino-acid sequence
J R Gentsch et al.
Journal of virology, 56(2), 356-364 (1985-11-01)
The effect of pretreatment of murine L cells with bacterial neuraminidases on type 3 reovirus attachment was examined. We observed that such treatments resulted in a 60 to 80% decrease of subsequent attachment of 35S-labeled type 3 reovirus in a
J Shemer et al.
Diabetologia, 29(5), 321-329 (1986-05-01)
Specific insulin receptors are present in the liver and brain of the lizard Anolis carolinesis. In this study, the specific binding of 125I-insulin to the receptors showed time, temperature and pH dependency. Specific binding to crude membranes prepared from brain
Emi Yamaguchi et al.
Journal of gastroenterology and hepatology, 22(7), 1134-1140 (2007-07-05)
The authors' previous report revealed that endothelin-1 might be released from B lymphocytes in cirrhotic patients with hypersplenism. Other investigators have shown that persistent exposure to environmental contaminants including arsenic might induce idiopathic portal hypertension. The aim of this study
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service