Millipore Sigma Vibrant Logo
Attention: We have moved. Merck Millipore products are no longer available for purchase on MerckMillipore.com.Learn More

324725 Endoglycosidase F1, Elizabethkingia meningosepticum, Recombinant, E. coli

View Products on Sigmaaldrich.com
324725
Purchase on Sigma-Aldrich

Overview

Replacement Information

Products

Catalogue NumberPackaging Qty/Pack
324725-700MIUCN 玻璃瓶 700 miu
Description
OverviewRecombinant, Elizabethkingia meningosepticum endoglycosidase F1 expressed in E. coli. Cleaves asparagine-linked or free oligomannose and hybrid, but not complex oligosaccharides. Core fucosylation reduces activity by 50 fold. Endo F1 will hydrolyze sulfate containing high mannose chains. 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.
Note: 1 mU = 1 milliunit.
Catalogue Number324725
Brand Family Calbiochem®
SynonymsEndo-β-N-acetylglucosaminidase F1, Endo F1
References
ReferencesTarentino, A.L., and Plummer, T.H. 1994. Methods Enzymol. 230, 44.
Tarentino, A.L., et al. 1992. J. Biol. Chem. 267, 3868.
Trimble, R.B., and Tarentino, A.L. 1991. J. Biol. Chem. 266, 1646.
Product Information
Activity≥17 units/ml
Unit of DefinitionOne unit is defined as the amount of enzyme that will release N-linked oligosaccharides from 1.0 µmol denatured ribonuclease B per min at 37°C, pH 5.5.
EC number3.2.1.96
FormLiquid
FormulationIn 20 mM Tris-HCl, pH 7.5.
Quality LevelMQ100
Applications
Biological Information
Specific Activity≥16 units/mg protein
Physicochemical Information
ContaminantsProteases: 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
Catalogue Number GTIN
324725-700MIUCN 04055977215991

Documentation

Endoglycosidase F1, Elizabethkingia meningosepticum, Recombinant, E. coli MSDS

Title

Safety Data Sheet (SDS) 

Endoglycosidase F1, Elizabethkingia meningosepticum, Recombinant, E. coli Certificates of Analysis

TitleLot Number
324725

References

Reference overview
Tarentino, A.L., and Plummer, T.H. 1994. Methods Enzymol. 230, 44.
Tarentino, A.L., et al. 1992. J. Biol. Chem. 267, 3868.
Trimble, R.B., and Tarentino, A.L. 1991. J. Biol. Chem. 266, 1646.

Citations

Title
  • Emily M. Kwan, et al. (2005) N-Glycosidase-carbohydrate-binding module fusion proteins as immobilized enzymes for protein deglycosylation. Protein Engineering Design and Selection 18, 497-501.
  • 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-September-2007 RFH
    SynonymsEndo-β-N-acetylglucosaminidase F1, Endo F1
    DescriptionRecombinant, Elizabethkingia meningosepticum endoglycosidase F1 expressed in E. coli. Cleaves asparagine-linked or free oligomannose and hybrid, but not complex oligosaccharides. Core fucosylation reduces activity by 50 fold. Endo F1 will hydrolyze sulfate containing high mannose chains. 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 20 mM Tris-HCl, pH 7.5.
    Recommended reaction conditions50 mM sodium phosphate buffer, pH 5.5
    EC number3.2.1.96
    ContaminantsProteases: none detected.
    Specific activity≥16 units/mg protein
    Activity≥17 units/ml
    Unit definitionOne unit is defined as the amount of enzyme that will release N-linked oligosaccharides from 1.0 µmol denatured ribonuclease B per min at 37°C, pH 5.5.
    Storage +2°C to +8°C
    Do Not Freeze Yes
    Toxicity Standard Handling
    ReferencesTarentino, A.L., and Plummer, T.H. 1994. Methods Enzymol. 230, 44.
    Tarentino, A.L., et al. 1992. J. Biol. Chem. 267, 3868.
    Trimble, R.B., and Tarentino, A.L. 1991. J. Biol. Chem. 266, 1646.
    Citation
  • Emily M. Kwan, et al. (2005) N-Glycosidase-carbohydrate-binding module fusion proteins as immobilized enzymes for protein deglycosylation. Protein Engineering Design and Selection 18, 497-501.