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317639 Dipeptidylpeptidase IV, His•Tag®, Human, Recombinant, S. frugiperda

317639
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317639-5MIU
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      Description
      OverviewRecombinant, human DPP IV fused at the N-terminus to a His•Tag® sequence and expressed in S. frugiperda insect cells. A serine exopeptidase dimer composed of two identical subunits of 110-130 kDa. DPPIV is involved in many cellular processes such as activation of cytokines, differentiation, and cell-matrix interactions. Inhibition of DPPIV has been reported to be an effective treatment for type II diabetes. Note: 1 mU = 1 milliunit.
      Note: 1 mU = 1 milliunit.
      Catalogue Number317639
      Brand Family Calbiochem®
      SynonymsCD26, DPPIV
      References
      ReferencesPospisilik, JA, et al. 2003. Diabetes 52, 741.
      Dobers, J., et al. 2002. Protein Expr. Purif. 25, 527.
      Marguet, D., et al. 2000. Proc. Natl. Acad. Sci. 97, 6874.
      Misumi, Y., et al. 1992. Biochim. Biophys. Acta 1131, 333.
      Product Information
      Unit of DefinitionOne unit is defined as the amount of enzyme that will hydrolyze 1 µmole H-Gly-Pro-AMC per min at 37°C, pH 8.0.
      EC number3.4.14.5
      FormLiquid
      FormulationIn 20 mM Tris-HCl, 5 mM CaCl₂, 1 µM ZnCl₂, 0.05% NaN₃, pH 8.0.
      Quality LevelMQ100
      Applications
      Biological Information
      Purity≥90% by SDS-PAGE
      Specific Activity≥8 U/mg protein
      Concentration Label Please refer to vial label for lot-specific concentration
      Physicochemical Information
      Dimensions
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Storage and Shipping Information
      Ship Code Dry Ice Only
      Toxicity Standard Handling
      Storage ≤ -70°C
      Avoid freeze/thaw Avoid freeze/thaw
      Do not freeze Ok to freeze
      Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C).
      Packaging Information
      Transport Information
      Supplemental Information
      Specifications

      Documentation

      Dipeptidylpeptidase IV, His•Tag®, Human, Recombinant, S. frugiperda FDS

      Titre

      Fiche de données de sécurité des matériaux (FDS) 

      Dipeptidylpeptidase IV, His•Tag®, Human, Recombinant, S. frugiperda Certificats d'analyse

      TitreNuméro de lot
      317639

      Références bibliographiques

      Aperçu de la référence bibliographique
      Pospisilik, JA, et al. 2003. Diabetes 52, 741.
      Dobers, J., et al. 2002. Protein Expr. Purif. 25, 527.
      Marguet, D., et al. 2000. Proc. Natl. Acad. Sci. 97, 6874.
      Misumi, Y., et al. 1992. Biochim. Biophys. Acta 1131, 333.
      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.

      Revision17-May-2010 JSW
      SynonymsCD26, DPPIV
      DescriptionRecombinant, human DPP IV fused at the N-terminus to a His•Tag® sequence and expressed in S. frugiperda insect cells. A serine exopeptidase dimer composed of two identical subunits of 110-130 kDa. DPPIV is involved in many cellular processes such as activation of cytokines, differentiation, and cell-matrix interactions. Inhibition of DPPIV has been reported to be an effective treatment for type II diabetes. Note: 1 mU = 1 milliunit.
      FormLiquid
      FormulationIn 20 mM Tris-HCl, 5 mM CaCl₂, 1 µM ZnCl₂, 0.05% NaN₃, pH 8.0.
      Concentration Label Please refer to vial label for lot-specific concentration
      EC number3.4.14.5
      Purity≥90% by SDS-PAGE
      Specific activity≥8 U/mg protein
      Unit definitionOne unit is defined as the amount of enzyme that will hydrolyze 1 µmole H-Gly-Pro-AMC per min at 37°C, pH 8.0.
      Storage ≤ -70°C
      Avoid freeze/thaw
      Do Not Freeze Ok to freeze
      Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C).
      Toxicity Standard Handling
      ReferencesPospisilik, JA, et al. 2003. Diabetes 52, 741.
      Dobers, J., et al. 2002. Protein Expr. Purif. 25, 527.
      Marguet, D., et al. 2000. Proc. Natl. Acad. Sci. 97, 6874.
      Misumi, Y., et al. 1992. Biochim. Biophys. Acta 1131, 333.