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Merck
CN

72197

Sigma-Aldrich

Neuraminidase from Vibrio cholerae

≥1.5 U/mL, specific activity ≥ 1.5U/mg protein

Synonym(s):

Acyl-neuraminyl Hydrolase, Receptor-destroying enzyme, Sialidase

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About This Item

CAS Number:
EC Number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
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biological source

Vibrio cholerae

form

liquid

specific activity

≥1.5 U/mg protein

concentration

≥1.5 U/mL

density

1.00 g/mL at 20 °C

storage temp.

2-8°C

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Application

Neurminidase is used as a cell-surface probe for glycoconjugate distribution and in substrate specificity studies.

Other Notes

1 U corresponds to the amount of enzyme which releases 1 μmol N-acetylneuraminic acid per minute at pH 4.5 and 37 °C (Neu5Acα(2-3,6)Galβ(1-4)Glc as substrate)
As a cell-surface probe of glycoconjugate distribution; Substrate specificity studies

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

高风险级别生物产品--病毒,疫苗等
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A K Shukla et al.
Analytical biochemistry, 158(1), 158-164 (1986-10-01)
A rapid and sensitive assay by high-performance liquid chromatography for determination of the activity and substrate specificity of sialidase (EC 3.2.1.18) and N-acetylneuraminate lyase (EC 4.1.3.3) is described. Sialic acids were separated on a strong anion-exchange resin using 0.75 mM
Bo Ram Kim et al.
Journal of enzyme inhibition and medicinal chemistry, 33(1), 1256-1265 (2018-08-22)
Sialidases are key virulence factors that remove sialic acid from the host cell surface glycan, unmasking receptors that facilitate bacterial adherence and colonisation. In this study, we developed potential agents for treating bacterial infections caused by Streptococcus pneumoniae Nan A
S W Whiteheart et al.
Analytical biochemistry, 163(1), 123-135 (1987-05-15)
Rat liver beta-galactoside alpha-2,6-sialyltransferase and Vibrio cholerae sialidase were used, in conjunction with CMP-N-acetyl-[3H]neuraminic acid, to probe the glycoconjugate distribution, sialylation state, and level of penultimate Gal beta 1-4GlcNAc residues on the surfaces of murine thymic lymphocytes. We report a
Kao-Tan Chen et al.
Zhongguo Zhong yao za zhi = Zhongguo zhongyao zazhi = China journal of Chinese materia medica, 37(20), 3068-3073 (2013-01-15)
To isolate and identify active neuraminidase constituents of Polygonum cuspidatum against influenza A (H1N1) influenza virus. On the basis of the bioassay-guided fractionation,such chromatographic methods as silica gel, sephadex LH-20 and HPLC were adopted to isolate active constituents of extracts
Johan Nordholm et al.
The Journal of biological chemistry, 288(15), 10652-10660 (2013-03-01)
Interactions that facilitate transmembrane domain (TMD) dimerization have been identified mainly using synthetic TMDs. Here, we investigated how inherent properties within natural TMDs modulate their interaction strength by exploiting the sequence variation in the nine neuraminidase subtypes (N1-N9) and the

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