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480708 α2-3,6-Neuraminidase, Clostridium perfringens, Recombinant, E. coli

480708
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Overview

Replacement Information

Products

Catalogue NumberPackaging Qty/Pack
480708-500MIU Plastic ampoule 500 miu
Description
OverviewRecombinant, Clostridium perfringens α2-3,6-Neuraminidase expressed in E. coli. Catalyzes the hydrolysis of non-reducing terminal α2,3 and α2,6 unbranched sialic acid residues from complex carbohydrates and glycoproteins. This enzyme does not exhibit activity on α2,8 or branched sialic acids.
Note: 1 mU = 1 milliunit.
Catalogue Number480708
Brand Family Calbiochem®
SynonymsAcetylneuraminyl Hydrolase, Sialidase
References
ReferencesPrime, S., et al. 1996. J. Chromatogr. A. 720, 263.
Dwek, R.A., et al. 1993. Annu. Rev. Biochem. 62, 65.
Ohta, Y., et al. 1989. J. Biochem (Tokyo) 106, 1086.
Product Information
CAS number9001-67-6
Activity≥10 units/ml
Unit of DefinitionOne unit is defined as the amount of enzyme that will catalyze the release of 1 µmol of methylumbelliferone from 2ʹ-(4-Methylumbelliferyl)-α-D-N-acetylneuraminic Acid (Cat. No. 474495) per min at 37°C, pH 5.0.
EC number3.2.1.18
FormLiquid
FormulationIn 25 mM NaCl, 20 mM Tris-HCl, pH 7.5.
Quality LevelMQ100
Applications
Biological Information
Specific Activity≥250 units/mg protein
Physicochemical Information
ContaminantsN-acetylglucosaminidase, α-fucosidase, α- and β-galactosidase, α- and β-mannosidase, proteases: none detected. Recommended reaction buffer: 50 mM sodium phosphate buffer, pH 6.0
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
RTECSQQ3450000
Safety Information
R PhraseR: 20-36/37/38-42/43

Harmful by inhalation.
Irritating to eyes, respiratory system and skin.
May cause sensitization by inhalation and skin contact.
S PhraseS: 26-36

In case of contact with eyes, rinse immediately with plenty of water and seek medical advice.
Wear suitable protective clothing.
Product Usage Statements
Storage and Shipping Information
Ship Code Blue Ice Only
Toxicity Harmful
Storage +2°C to +8°C
Do not freeze Yes
Packaging Information
Transport Information
Supplemental Information
Specifications

Documentation

α2-3,6-Neuraminidase, Clostridium perfringens, Recombinant, E. coli SDS

Title

Safety Data Sheet (SDS) 

α2-3,6-Neuraminidase, Clostridium perfringens, Recombinant, E. coli Certificates of Analysis

TitleLot Number
480708

References

Reference overview
Prime, S., et al. 1996. J. Chromatogr. A. 720, 263.
Dwek, R.A., et al. 1993. Annu. Rev. Biochem. 62, 65.
Ohta, Y., et al. 1989. J. Biochem (Tokyo) 106, 1086.
Data Sheet

Note that this data sheet is not lot-specific and is representative of the current specifications for this product. Please consult the vial label and the certificate of analysis for information on specific lots. Also note that shipping conditions may differ from storage conditions.

Revision11-August-2008 RFH
SynonymsAcetylneuraminyl Hydrolase, Sialidase
DescriptionRecombinant, Clostridium perfringens α2-3,6-Neuraminidase expressed in E. coli. Catalyzes the hydrolysis of non-reducing terminal α2,3 and α2,6 unbranched sialic acid residues from complex carbohydrates and glycoproteins. This enzyme does not exhibit activity on α2,8 or branched sialic acids.
FormLiquid
FormulationIn 25 mM NaCl, 20 mM Tris-HCl, pH 7.5.
Recommended reaction conditions50 mM sodium phosphate buffer, pH 6.0.
CAS number9001-67-6
RTECSQQ3450000
EC number3.2.1.18
ContaminantsN-acetylglucosaminidase, α-fucosidase, α- and β-galactosidase, α- and β-mannosidase, proteases: none detected. Recommended reaction buffer: 50 mM sodium phosphate buffer, pH 6.0
Specific activity≥250 units/mg protein
Activity≥10 units/ml
Unit definitionOne unit is defined as the amount of enzyme that will catalyze the release of 1 µmol of methylumbelliferone from 2ʹ-(4-Methylumbelliferyl)-α-D-N-acetylneuraminic Acid (Cat. No. 474495) per min at 37°C, pH 5.0.
Storage +2°C to +8°C
Do Not Freeze Yes
Toxicity Harmful
ReferencesPrime, S., et al. 1996. J. Chromatogr. A. 720, 263.
Dwek, R.A., et al. 1993. Annu. Rev. Biochem. 62, 65.
Ohta, Y., et al. 1989. J. Biochem (Tokyo) 106, 1086.