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10269611001

Roche

Neuraminidase (Sialidase)

from Arthrobacter ureafaciens

Synonym(s):

PCR, taq

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1 unit

Available to ship TODAYfromMILWAUKEE

$409.00

About This Item

UNSPSC Code:
12352204
EC Number:
NACRES:
NA.54
Specific activity:
~25 units/mg protein
Biological source:
bacterial (Arthrobacter ureafaciens)

$409.00


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biological source

bacterial (Arthrobacter ureafaciens)

form

solution

specific activity

~25 units/mg protein

packaging

pkg of 1 U (100 μl)

manufacturer/tradename

Roche

optimum pH

5.0-5.5

storage temp.

2-8°C

General description

Neuraminidase hydrolyzes terminal N- or O-acylneuraminic acids which are α2,3-, α2,6-, or α2,8-linked (rate: α2,6 > α2,3 > α2,8) to oligosaccharides, polysaccharides, mucopolysaccharides, glycoproteins, and glycolipids. Noteworthy, for the hydrolysis of glycolipids, the presence of a detergent is necessary. Because of the broad substrate specificity, the enzyme is very well suited for the complete removal of sialic acids from glycoconjugates of a wide variety of biological materials.[1]
This product is a mixture of isoenzymes (L, M1, M2 and S) with the following molecular weight values: ~ 52 kDa, 66 kDa and 88 kDa.

Application

For the hydrolysis of glycolipids, the presence of a detergent is necessary. Because of the broad substrate specificity, the enzyme is very well suited for the complete removal of sialic acids from glycoconjugates of a wide variety of biological materials.
Neuraminidase has been used for the:
  • detection of the cell surface glycosylations in human anaplastic large cell lymphoma cells[2]
  • release of sialic acid from cells[3]
  • antibody-overlay lectin microarray[4]
  • cell surface lectin array analysis.[2][4]
  • hemagglutination assays.
  • cell adhesion assay.

Biochem/physiol Actions

Cleaves terminal sialic-acid residues that are α2,3-, α2,6-, or α2,8-linked to Gal, GlcNAc, GalNAc, AcNeu, GlcNeu, oligosaccharides, glycolipids, or glycoproteins. Relative rate of cleavage is α2,6 >α2,3 >α2,8, determined on bonds in tri- and tetrasaccharides.

Physical form

Solution in 10 mM sodium phosphate, 0.1% Micr-O-Protect (w/v), 0.25 mg/ml bovine serum albumin, pH 7

Preparation Note

Working concentration: Enzyme/substrate ratio should be in the range of 0.04 U/25-80 μg.

Other Notes

For life science research only. Not for use in diagnostic procedures.

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This Item
1108072500111585886001N7885
biological source

bacterial (Arthrobacter ureafaciens)

biological source

Vibrio cholerae

biological source

bacterial (Clostridium perfringens)

biological source

-

specific activity

~25 units/mg protein

specific activity

-

specific activity

100 U/mg, ~100 units/mg protein

specific activity

1-5 units/mg protein (Lowry, using NAN-lactose)

form

solution

form

solution

form

lyophilized

form

buffered aqueous solution

optimum pH

5.0-5.5

optimum pH

5.5-6.2

optimum pH

5

optimum pH

-

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

manufacturer/tradename

Roche

manufacturer/tradename

Roche

manufacturer/tradename

Roche

manufacturer/tradename

-


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Protocols

Neuraminidase can be used to cleave sialic acids from proteins. In this protocol, the enzyme from Vibrio cholerae is used on fixed cells.


Charting the Proteoform Landscape of Serum Proteins in Individual Donors by High-Resolution Native Mass Spectrometry.
Cramer, et al.
Analytical Chemistry, 94, 12732-12741 (2022)
Sialylation by ??galactoside ??2,6?sialyltransferase and N?glycans regulate cell adhesion and invasion in human anaplastic large cell lymphoma
Suzuki O, et al.
International Journal of Oncology, 46(3), 973-980 (2015)
Jiaqi Wu et al.
BioTechniques, 68(2), 85-90 (2020-01-16)
Carbohydrate-deficient transferrin (CDT) is a reliable biomarker for chronic alcohol abuse. We developed a method for CDT analysis by capillary isoelectric focusing, followed by immunodetection directly in the capillary, in an automated fashion and on a single platform (Peggy Sue™;



Global Trade Item Number

SKUGTIN
1026961100104061838250513