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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-624-6
MDL number:
Product Name
Neuraminidase from Vibrio cholerae, Type II, buffered aqueous solution, 8-24 units/mg protein (Lowry, using NAN-lactose)
biological source
Vibrio cholerae
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
Quality Level
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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.
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.
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.
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.
Analysis Note
Preservative free.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
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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Increase of leukemia L1210 immunogenicity by Vibrio cholerae neuraminidase treatment.
J G Bekesi et al.
Cancer research, 31(12), 2130-2132 (1971-12-01)
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.
Viruses, 12(10) (2020-10-24)
Polyomaviruses are small, non-enveloped DNA tumor viruses that cause serious disease in immunosuppressed people, including progressive multifocal leukoencephalopathy (PML) in patients infected with JC polyomavirus, but the molecular events mediating polyomavirus entry are poorly understood. Through genetic knockdown approaches, we
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
Matthew D Lauver et al.
eLife, 9 (2020-09-18)
JCPyV polyomavirus, a member of the human virome, causes progressive multifocal leukoencephalopathy (PML), an oft-fatal demyelinating brain disease in individuals receiving immunomodulatory therapies. Mutations in the major viral capsid protein, VP1, are common in JCPyV from PML patients (JCPyV-PML) but
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