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

324725
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      Overview

      Replacement Information

      Key Specifications Table

      Pricing & Availability

      Catalog NumberAvailability Packaging Qty/Pack Price Quantity
      324725-700MIU
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          Glass bottle 700 miu
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          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.
          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

          Documentation

          SDS

          Title

          Safety Data Sheet (SDS) 

          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.