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219555 Cathepsin K Substrate II, Fluorogenic - Calbiochem

An internally quenched, highly cathepsin K-selective, fluorogenic peptide substrate that is efficiently cleaved by CatK (kcat/Km = 0.426 µM⁻¹ S⁻¹), but not by Cathepsins B/L/S/F/H/V.

FDS (Fiches de données de sécurité), certificats d’analyse (CoA) et de qualité (CoQ), dossiers, brochures et autres documents disponibles.

Synonymes: Abz-HPG~GPQ-EDN₂ph

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219555
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219555-1MG
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      Description
      OverviewAn internally quenched, highly cathepsin K-selective, fluorogenic peptide substrate that is efficiently cleaved by CatK (kcat/Km = 0.426 µM-1 S-1), but not by Cathepsins B/L/S/F/H/V. Studies using WT and CatK-/- mice reveal that the substrate is not cleaved by other proteolytic enzymes present in fibroblast lysates.
      Catalogue Number219555
      Brand Family Calbiochem®
      SynonymsAbz-HPG~GPQ-EDN₂ph
      References
      ReferencesLecaille, F., et al. 2003. Biochem. J. 375, 307.
      Product Information
      FormBright yellow solid
      FormulationSupplied as a trifluoroacetate salt.
      Hill FormulaC₄₀H₅₀N₁₄O₁₂
      Chemical formulaC₄₀H₅₀N₁₄O₁₂
      Hygroscopic Hygroscopic
      Structure formula ImageStructure formula Image
      Quality LevelMQ100
      Applications
      Biological Information
      Purity≥95% by HPLC
      Physicochemical Information
      Emission max.
      Excitation max.
      Peptide SequenceAbz-His-Pro-Gly~Gly-Pro-Gln-EDDnp
      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
      Protect from Light Protect from light
      Protect from Moisture Protect from moisture
      Hygroscopic Hygroscopic
      Do not freeze Ok to freeze
      Special InstructionsFollowing reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 3 months at -20°C.
      Packaging Information
      Packaged under inert gas Packaged under inert gas
      Transport Information
      Supplemental Information
      Specifications
      Global Trade Item Number
      Référence GTIN
      219555-1MG 04055977218114

      Documentation

      Cathepsin K Substrate II, Fluorogenic - Calbiochem FDS

      Titre

      Fiche de données de sécurité des matériaux (FDS) 

      Cathepsin K Substrate II, Fluorogenic - Calbiochem Certificats d'analyse

      TitreNuméro de lot
      219555

      Références bibliographiques

      Aperçu de la référence bibliographique
      Lecaille, F., et al. 2003. Biochem. J. 375, 307.
      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.

      Revision25-August-2009 RFH
      SynonymsAbz-HPG~GPQ-EDN₂ph
      DescriptionAn internally quenched, highly cathepsin K-selective, fluorogenic peptide substrate that is efficiently cleaved by CatK (kcat/Km = 0.426 µM-1 S-1), but not by Cathepsins B/L/S/F/H/V. Studies using WT and CatK-/- mice reveal that the substrate is not cleaved by other proteolytic enzymes present in fibroblast lysates. Emission Max: 420 NM, Excitation Max: 320 nM.
      FormBright yellow solid
      FormulationSupplied as a trifluoroacetate salt.
      Intert gas (Yes/No) Packaged under inert gas
      Chemical formulaC₄₀H₅₀N₁₄O₁₂
      Peptide SequenceAbz-His-Pro-Gly~Gly-Pro-Gln-EDDnp
      Structure formulaStructure formula
      Purity≥95% by HPLC
      SolubilityDMSO (5 mg/ml)
      Storage Protect from moisture
      Protect from light
      -20°C
      Hygroscopic
      Do Not Freeze Ok to freeze
      Special InstructionsFollowing reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 3 months at -20°C.
      Toxicity Standard Handling
      ReferencesLecaille, F., et al. 2003. Biochem. J. 375, 307.