72197
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:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-624-6
MDL number:
Specific activity:
≥1.5 U/mg protein
Biological source:
Vibrio cholerae
Concentration:
≥1.5 U/mL
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
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
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signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
高风险级别生物产品--病毒，疫苗等
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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
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