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324726 Endoglycosidase F2, Elizabethkingia meningosepticum, Recombinant, E. coli

324726
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概述

Replacement Information

Products

产品目录编号包装 数量 / 包装
324726-200MIUCN 塑胶安瓿;塑胶针药瓶 200 miu
Description
OverviewRecombinant, Elizabethkingia meningosepticum endoglycosidase F2 expressed in E. coli. Cleaves asparagine-linked or free oligomannose and biantennary complex oligosaccharides from glycoproteins. It cleaves between the two N-acetylglucosamine residues in the diacetylchitobiose core of the oligosaccharide generating a truncated sugar molecule with one N-acetylglucosamine residue remaining on the asparagine. Less sensitive to protein conformation than N-Glycosidase F (Cat. No. 362185) and therefore is more suitable for deglycosylation of native proteins. This enzyme is not active above pH 6.0.
Note: 1 mU = 1 milliunit.
Catalogue Number324726
Brand Family Calbiochem®
SynonymsEndo-β-N-acetylglucosaminidase F2, Endo F2
References
ReferencesReddy, A., et al. 1998. Glycobiology 8, 633.
Tarentino, A.L., and Plummer, T.H. 1994. Methods Enzymol. 230, 44.
Tarentino, A.L., et al. 1993. J. Biol. Chem. 268, 9702.
Trimble, R.B., and Tarentino, A.L. 1991. J. Biol. Chem. 266, 1646.
Product Information
Activity≥5 units/ml
Unit of DefinitionOne unit is defined as the amount of enzyme that will release N-linked oligosaccharides from 1 µmol porcine fibrinogen per min at 37°C, pH 4.5.
EC number3.2.1.96
FormLiquid
FormulationIn 25 mM NaCl, 10 mM sodium acetate buffer, pH 4.5.
Quality LevelMQ100
Applications
Biological Information
Specific Activity≥20 units/mg protein
Physicochemical Information
ContaminantsN-acetylglucosaminidase, α- and β-galactosidase, α-mannosidase, neuraminidases, proteases: none detected
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Storage and Shipping Information
Ship Code Blue Ice Only
Toxicity Standard Handling
Storage +2°C to +8°C
Do not freeze Yes
Packaging Information
Transport Information
Supplemental Information
Specifications
Global Trade Item Number
产品目录编号 GTIN
324726-200MIUCN 04055977216004

Documentation

Endoglycosidase F2, Elizabethkingia meningosepticum, Recombinant, E. coli MSDS

职位

物料安全数据表 (MSDS) 

Endoglycosidase F2, Elizabethkingia meningosepticum, Recombinant, E. coli 分析证书

标题批号
324726

参考

参考信息概述
Reddy, A., et al. 1998. Glycobiology 8, 633.
Tarentino, A.L., and Plummer, T.H. 1994. Methods Enzymol. 230, 44.
Tarentino, A.L., et al. 1993. J. Biol. Chem. 268, 9702.
Trimble, R.B., and Tarentino, A.L. 1991. J. Biol. Chem. 266, 1646.
数据表

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-September-2007 RFH
SynonymsEndo-β-N-acetylglucosaminidase F2, Endo F2
DescriptionRecombinant, Elizabethkingia meningosepticum endoglycosidase F2 expressed in E. coli. Cleaves asparagine-linked or free oligomannose and biantennary complex oligosaccharides from glycoproteins. It cleaves between the two N-acetylglucosamine residues in the diacetylchitobiose core of the oligosaccharide generating a truncated sugar molecule with one N-acetylglucosamine residue remaining on the asparagine. Less sensitive to protein conformation than N-Glycosidase F (Cat. No. 362185) and therefore, is more suitable for deglycosylation of native proteins.
FormLiquid
FormulationIn 25 mM NaCl, 10 mM sodium acetate buffer, pH 4.5.
Recommended reaction conditions50 mM sodium acetate buffer, pH 4.5. (Note: enzyme is not active above pH 6.0)
EC number3.2.1.96
ContaminantsN-acetylglucosaminidase, α- and β-galactosidase, α-mannosidase, neuraminidases, proteases: none detected
Specific activity≥20 units/mg protein
Activity≥5 units/ml
Unit definitionOne unit is defined as the amount of enzyme that will release N-linked oligosaccharides from 1 µmol porcine fibrinogen per min at 37°C, pH 4.5.
Storage +2°C to +8°C
Do Not Freeze Yes
Toxicity Standard Handling
ReferencesReddy, A., et al. 1998. Glycobiology 8, 633.
Tarentino, A.L., and Plummer, T.H. 1994. Methods Enzymol. 230, 44.
Tarentino, A.L., et al. 1993. J. Biol. Chem. 268, 9702.
Trimble, R.B., and Tarentino, A.L. 1991. J. Biol. Chem. 266, 1646.