362180 N-Glycosidase A, Almond

362180
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      Prix & Disponibilité

      Référence DisponibilitéConditionnement Qté Prix Quantité
      362180-5MIU
      Récupération des données relatives à la disponibilité...
      Disponibilité limitéeDisponibilité limitée
      En stock 
      Interrompu(e)
      Disponible en quantités limitées
      Disponibilité à confirmer
        Pour le restant : Nous vous tiendrons informé
          Pour le restant : Nous vous tiendrons informé
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          Ampoule plast. 5 miu
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          Description
          OverviewNative N-Glycosidase A from almonds. Cleaves N-glycan chains from glycopeptides, including those with α1,3-linked core fucose. This enzyme cleaves between GlcNAc and asparagine.
          Note: 1 mU = 1 milliunit.
          Catalogue Number362180
          Brand Family Calbiochem®
          SynonymsGlycopeptidase A, PNGase A
          References
          ReferencesMeans, R.E. and Desrosiers, R.C. 2000. J. Virol. 74, 11181.
          Fan, J.Q., and Lee, Y.C. 1997. J. Biol. Chem. 272, 27058.
          Altmann, F., et al. 1995. Glycoconj. J. 12, 84.
          Takahashi, N., and Nishibe, H. 1978. J. Biochem. 84, 1467.
          Product Information
          CAS number83534-39-8
          Unit of DefinitionOne unit is defined as the amount of enzyme that will catalyze the release of 1.0 µmol hybrid and high-mannose oligosaccharides from ovalbumin glycopeptide per min at 37°C, pH 5.0.
          EC number3.5.1.52
          FormLiquid
          FormulationIn 50 mM citrate/phosphate buffer, 50% glycerol, pH 5.0.
          Quality LevelMQ100
          Applications
          Biological Information
          Specific Activity≥500 mU/mg protein
          Physicochemical Information
          Contaminantsα- and β-galactosidase, β-glucosidase: ≤0.1%; 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 -20°C
          Do not freeze Ok to freeze
          Special InstructionsFollowing initial thaw, aliquot and freeze (-20°C).
          Packaging Information
          Transport Information
          Supplemental Information
          Specifications

          Documentation

          N-Glycosidase A, Almond FDS

          Titre

          Fiche de données de sécurité des matériaux (FDS) 

          N-Glycosidase A, Almond Certificats d'analyse

          TitreNuméro de lot
          362180

          Références bibliographiques

          Aperçu de la référence bibliographique
          Means, R.E. and Desrosiers, R.C. 2000. J. Virol. 74, 11181.
          Fan, J.Q., and Lee, Y.C. 1997. J. Biol. Chem. 272, 27058.
          Altmann, F., et al. 1995. Glycoconj. J. 12, 84.
          Takahashi, N., and Nishibe, H. 1978. J. Biochem. 84, 1467.
          Fiche technique

          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.

          Revision13-September-2007 RFH
          SynonymsGlycopeptidase A, PNGase A
          DescriptionNative N-Glycosidase A from almonds. Cleaves N-glycan chains from glycopeptides, including those with α1,3-linked core fucose. This enzyme cleaves between GlcNAc and asparagine. Has an optimal pH of 4.0-6.0.
          FormLiquid
          FormulationIn 50 mM citrate/phosphate buffer, 50% glycerol, pH 5.0.
          Recommended reaction conditions
          Deglycosylation of Glycopeptides For assaying N-Glycosidase A Use 0.5 mU/ml N-Glycosidase A in 100 mM citrate / phosphate buffer, pH 5.0 with 0.1% BSA. Guideline used for unit definition: 10 µl of 100 µM ovalbumin glycopeptide was incubated with 10 µl 0.5 mU/ml N-Glycosidase A at 37°C for 60 min. Reaction products were quantified by absorption at 220 nm on reversed phase HPLC (5 µm ODS-Hypersil column) at 220 nm. For preparative digestion Incubate 0.2-0.5 mU N-Glycosidase A with 100 nmoles glycopeptide in 20-50 µl citrate/phosphate buffer without BSA for 24 hrs at 37°C. Deglycosylation of Glycoproteins Various reagents such as 0.75 M β-mercaptethanol, 2% Triton X-100, 2% Tween®-80 detergent may be required to denature substrates sufficiently for deglycosylation. Enzyme activity may be significantly increased by addition of Mg2+, Zn2+, Co3+, or Cu3+. A guideline is 4 µglycoprotein incubated with 1 mU N-Glycosidase A in 10 mM sodium acetate, 0.5 M NaSCN, 0.1 M β-mercaptoethanol, pH 5.1, for 24 h at 37°C. However the nature of the glycoprotein substrate will determine optimal conditions. References Taga, E.M. et al. 1984. Biochemistry 23, 815. Tarentino, A.L. and Plummer, T.H. 1982. J. Biol. Chem. 257, 10776. Takahashi, N. and Nishibe, H. 1981. Biochim. Biophys. Acta 657, 457
          CAS number83534-39-8
          EC number3.5.1.52
          Contaminantsα- and β-galactosidase, β-glucosidase: ≤0.1%; proteases: none detected
          Specific activity≥500 mU/mg protein
          Unit definitionOne unit is defined as the amount of enzyme that will catalyze the release of 1.0 µmol hybrid and high-mannose oligosaccharides from ovalbumin glycopeptide per min at 37°C, pH 5.0.
          Storage -20°C
          Do Not Freeze Ok to freeze
          Special InstructionsFollowing initial thaw, aliquot and freeze (-20°C).
          Toxicity Standard Handling
          ReferencesMeans, R.E. and Desrosiers, R.C. 2000. J. Virol. 74, 11181.
          Fan, J.Q., and Lee, Y.C. 1997. J. Biol. Chem. 272, 27058.
          Altmann, F., et al. 1995. Glycoconj. J. 12, 84.
          Takahashi, N., and Nishibe, H. 1978. J. Biochem. 84, 1467.