N6514
Neuraminidase from Vibrio cholerae
Type II, buffered aqueous solution, 8-24 units/mg protein (Lowry, using NAN-lactose)
Synonyme(s) :
Acyl-neuraminyl Hydrolase, Receptor-destroying enzyme, Sialidase
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A propos de cet article
Numéro CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-624-6
MDL number:
Specific activity:
8-24 units/mg protein (Lowry, using NAN-lactose)
Biological source:
Vibrio cholerae
Service technique
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Vibrio cholerae
Quality Level
type
Type II
form
buffered aqueous solution
specific activity
8-24 units/mg protein (Lowry, using NAN-lactose)
foreign activity
Protease and NAN-aldolase, present
storage temp.
2-8°C
General description
Calorimetry studies show that the two lectin-like domains flanking the central catalytic domain of Neuraminidase serve as the recognition and binding sites for sialic acid-containing substrates.
Neuraminidase enzymes are hydrolase enzymes that promote influenza virus release from infected cells and facilitate virus spread.
Application
Neurminidase is used as a cell-surface probe for glycoconjugate distribution and in substrate specificity studies.
Neuraminidase from Vibrio cholera has been used in a study to describe a five-step purification method. It has also been used in a study to investigate modification of leukemia L1210 tumor cells.
Physical form
Solution in 50 mM sodium acetate, pH 5.5, containing 0.15 M sodium chloride and 4 mM calcium chloride, 0.2 μm filtered..
Preparation Note
A further purification by affinity chromatography of our Type III.
Analysis Note
Preservative free.
Other Notes
One unit will liberate 1.0 μmole of N-acetylneuraminic acid per min at pH 5.0 at 37 °C using NAN-lactose or bovine submaxillary mucin, unless otherwise specified. Prices based on units using NAN-lactose as substrate.
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Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Classe de stockage
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Contenu apparenté
Ibrahim Moustafa et al.
The Journal of biological chemistry, 279(39), 40819-40826 (2004-07-01)
Vibrio cholerae neuraminidase (VCNA) plays a significant role in the pathogenesis of cholera by removing sialic acid from higher order gangliosides to unmask GM1, the receptor for cholera toxin. We previously showed that the structure of VCNA is composed of
Nicolas Burin des Roziers et al.
Transfusion, 55(6 Pt 2), 1563-1571 (2015-01-06)
Pneumococcal hemolytic uremic syndrome (P-HUS) is a rare but severe complication of invasive pneumococcal disease (IPD) in young children. Consensual biologic diagnosis criteria are currently lacking. A prospective study was conducted on 10 children with culture-confirmed IPD. Five presented with
S Crennell et al.
Structure (London, England : 1993), 2(6), 535-544 (1994-06-15)
Vibrio cholerae neuraminidase is part of a mucinase complex which may function in pathogenesis by degrading the mucin layer of the gastrointestinal tract. The neuraminidase, which has been the target of extensive inhibitor studies, plays a subtle role in the