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Merck

72197

Sigma-Aldrich

Neuraminidase from Vibrio cholerae

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

Sinónimos:

Acyl-neuraminyl Hydrolase, Receptor-destroying enzyme, Sialidase

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About This Item

Número de CAS:
Comisión internacional de enzimas:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

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.

Unit Definition

1 U entspricht der Enzymmenge, die 1 μmol N-Acetylneuraminsäure pro Minute bei pH 4.5 und 37°C freisetzt (Neu5Acα(2-3,6)Galβ(1-4)Glc als Substrat)

Other Notes

As a cell-surface probe of glycoconjugate distribution; Substrate specificity studies

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


Certificados de análisis (COA)

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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
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
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
Quanjiao Chen et al.
PloS one, 8(1), e54334-e54334 (2013-01-26)
Two surface glycoproteins of influenza virus, haemagglutinin (HA) and neuraminidase (NA), play opposite roles in terms of their interaction with host sialic acid receptors. HA attaches to sialic acid on host cell surface receptors to initiate virus infection while NA
Ramaiah Arunachalam et al.
Interdisciplinary sciences, computational life sciences, 4(4), 282-290 (2013-01-29)
The aim of the present investigation was to discover the genetic relationships of 2009 pandemic novel influenza A/H1N1 virus (NIV) external antigens Hemagglutinin (HA) and Neuraminidase (NA) with other influenza viruses by performing phylogenetic, comparative and statistical analyses. Phylogenetic trees

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