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PF113 ADAMTS4, Truncated, His•Tag®, Human, Recombinant, Insect Cells

Ficha de datos de seguridad (MSDS o SDS), certificado de análisis y de calidad (CoA y CoQ), expedientes, folletos y otros documentos disponibles.

Sinónimos: Aggrecanase 1

PF113
  
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      Descripción

      Replacement Information
      Description
      Overview

      This product has been discontinued.





      Recombinant, human, truncated ADAMTS4 (amino acids 213-579) fused at the C-terminus to a His•Tag® sequence and expressed in S. frugiperda insect cells using a baculovirus expression. ADAMTS4 (a disintegrin and metalloproteinase with thrombospondin motif-4) belongs to a novel family of extracellular proteinases that hydrolyze aggrecan, the major proteoglycan of articular cartilage. Useful for the study of extracellular proteoglycan degradation, screening for inhibitors of proteoglycan hydrolysis, and as a standard in enzymatic and immunochemical assays.
      Catalogue NumberPF113
      Brand Family Calbiochem®
      SynonymsAggrecanase 1
      References
      ReferencesTang, B.L., et al. 2001. Int. J. Biochem. 33, 33.
      Tortorella, M.D., et al. 2000. J. Biol. Chem. 275, 18566.
      Tortorella, M.D., et al. 1999. Science 284, 1664.
      Product Information
      Unit of DefinitionOne unit is defined as the amount of enzyme necessary to hydrolyze 1.0 nmol of recombinant aggrecan interglobular domain (Cat. No. PF114) per min at 37°C, pH 7.5.
      FormLiquid
      FormulationIn 150 mM NaCl, 50 mM Tris-HCl, 5 mM CaCl₂, 0.05% BRIJ® 35 Detergent, pH 7.5.
      PreservativeNone
      Applications
      Biological Information
      Purity≥90% by SDS-PAGE
      Specific Activity≥1.5 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
      Global Trade Item Number
      Número de referencia GTIN
      PF113 0

      Documentation

      ADAMTS4, Truncated, His•Tag®, Human, Recombinant, Insect Cells Certificados de análisis

      CargoNúmero de lote
      PF113

      Referencias bibliográficas

      Visión general referencias
      Tang, B.L., et al. 2001. Int. J. Biochem. 33, 33.
      Tortorella, M.D., et al. 2000. J. Biol. Chem. 275, 18566.
      Tortorella, M.D., et al. 1999. Science 284, 1664.
      Ficha técnica

      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.

      Revision18-April-2012 JSW
      SynonymsAggrecanase 1
      DescriptionRecombinant, human, truncated ADAMTS4 (amino acids 213-579) fused at the C-terminus to a His•Tag® sequence and expressed in S. frugiperda insect cells using a baculovirus expression. Due to autoproteolytic activity, minor bands may be visible in the enzyme preparation.
      ADAMTS4 (A Disintegrin And Metalloproteinase with Thrombospondin motif-4) is a ~68 kDa protein belonging to a novel family of extracellular proteinases that hydrolyze aggrecan, the major proteoglycan of articular cartilage. Two other members of the ADAMTS family, ADAMTS1 and ADAMTS5, also will digest aggrecan, and aggrecan degradation products are found in normal and rheumatoid or osteoarthritic joint cartilage as a result of the action of any of these 3 proteases. ADAMTS4 hydrolyzes aggrecan at 5 different cleavage sites, including 4 in the chondroitin sulfate-rich region between globular domains G2 and G3, and another site in the rod-shaped polypeptide between globular domains G1 and G2. ADAMTS4 also hydrolyzes other lecticans such as brevican and versican. ADAMTS4 activity is inhibited by TMP-3 (ki in the nM range) and to a lesser extent by other TIMP proteins. Activity is alsosuppressed by chelators of divalent cations such as EDTA and by synthetic metalloproteinase inhibitors.
      BackgroundADAMTS4 (A Disintegrin And Metalloproteinase with Thrombospondin motif-4) is a ~68 kDa protein belonging to a novel family of extracellular proteinases that hydrolyze aggrecan, the major proteoglycan of articular cartilage. Two other members of the ADAMTS family, ADAMTS1 and ADAMTS5, also will digest aggrecan, and aggrecan degradation products are found in normal and rheumatoid or osteoarthritic joint cartilage as a result of the action of any of these 3 proteases. ADAMTS4 hydrolyzes aggrecan at 5 different cleavage sites, including 4 in the chondroitin sulfate-rich region between globular domains G2 and G3, and another site in the rod-shaped polypeptide between globular domains G1 and G2. ADAMTS4 also hydrolyzes other lecticans such as brevican and versican.
      FormLiquid
      FormulationIn 150 mM NaCl, 50 mM Tris-HCl, 5 mM CaCl₂, 0.05% BRIJ® 35 Detergent, pH 7.5.
      Concentration Label Please refer to vial label for lot-specific concentration
      Purity≥90% by SDS-PAGE
      Specific activity≥1.5 U/mg protein
      Unit definitionOne unit is defined as the amount of enzyme necessary to hydrolyze 1.0 nmol of recombinant aggrecan interglobular domain (Cat. No. PF114) per min at 37°C, pH 7.5.
      PreservativeNone
      Storage Avoid freeze/thaw
      ≤ -70°C
      Do Not Freeze Ok to freeze
      Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C).
      Toxicity Standard Handling
      ReferencesTang, B.L., et al. 2001. Int. J. Biochem. 33, 33.
      Tortorella, M.D., et al. 2000. J. Biol. Chem. 275, 18566.
      Tortorella, M.D., et al. 1999. Science 284, 1664.