N6514
Neuraminidase from Vibrio cholerae
Type II, buffered aqueous solution, 8-24 units/mg protein (Lowry, using NAN-lactose)
Synonym(s):
Acyl-neuraminyl Hydrolase, Receptor-destroying enzyme, Sialidase
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About This Item
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biological source
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
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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
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.
Neurminidase is used as a cell-surface probe for glycoconjugate distribution and in substrate specificity studies.
Quality
Preservative free.
Unit Definition
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.
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.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
10 - Combustible liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Increase of leukemia L1210 immunogenicity by Vibrio cholerae neuraminidase treatment.
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Hirokazu Kai et al.
Bioorganic & medicinal chemistry, 20(8), 2739-2746 (2012-03-14)
A selective and potent inhibitor of neuraminidases, a hydrolase that is responsible for processing sialylated glycoconjugates, is a promising drug candidate for various infective diseases. The current study demonstrates that the use of an aglycone-focused library of 2-difluoromethylphenyl α-sialosides is
Paul Clark et al.
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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
Julia Moh-Klaren et al.
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Red blood cell (RBC) Thomsen-Friedenreich antigen exposure (T activation) in infants with necrotizing enterocolitis (NEC) has occasionally been associated with posttransfusional intravascular hemolysis thought to be due to anti-T antibodies in the donor plasma. We describe an infant with NEC
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