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444279 InnoZyme™ Gelatinase Substrate, Fluorogenic

444279
  
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      Aperçu

      Replacement Information
      Description
      Overview

      This product has been discontinued.





      An internally quenched fluorogenic peptide substrate that undergoes selective hydrolysis by MMP-2 and MMP-9 (kcat/KM = 14,002 s-1M-1 and 5,499 s-1M-1, respectively) at the Gly~Val bond. The peptide substrate is designed from the five triple-helical collagen sequence hydrolyzed by MMP-9. Very weakly recognizes MMP-1, MMP-3, MMP-13, and MMP-14 activities (kcat/KM < 600 s-1M-1). Displays thermal stability and aqueous solubility. Also useful for continuously monitoring MMP triple helical peptidase (THP) activities.
      Catalogue Number444279
      Brand Family Calbiochem®
      SynonymsGelatinase A/Gelatinase B Substrate III, α1(V)436-447 fTHP, H-(GPHyp)₅-GPK(Mca)-GPPG~VVGEK(Dnp)-GEQ-(GPHyp)₅-NH₂
      References
      ReferencesLauer-Fields, J.L., et al. 2003. J. Biol. Chem. 278, 18140.
      Product Information
      FormYellow solid
      FormulationSupplied as a trifluoroacetate salt.
      Hill FormulaC₂₀₀H₂₈₃N₅₁O₆₈
      Chemical formulaC₂₀₀H₂₈₃N₅₁O₆₈
      Hygroscopic Hygroscopic
      Applications
      Biological Information
      Purity≥95% by HPLC
      Physicochemical Information
      Peptide SequenceH₂N-(Gly-Pro-Hyp)₅-Gly-Pro-Lys(Mca)-Gly-Pro-Pro-Gly~Val-Val-Gly-Glu-Lys(Dnp)-Gly-Glu-Gln-(Gly-Pro-Hyp)₅-NH₂
      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
      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
      444279 0

      Documentation

      InnoZyme™ Gelatinase Substrate, Fluorogenic Certificats d'analyse

      TitreNuméro de lot
      444279

      Références bibliographiques

      Aperçu de la référence bibliographique
      Lauer-Fields, J.L., et al. 2003. J. Biol. Chem. 278, 18140.
      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.

      Revision07-August-2008 RFH
      SynonymsGelatinase A/Gelatinase B Substrate III, α1(V)436-447 fTHP, H-(GPHyp)₅-GPK(Mca)-GPPG~VVGEK(Dnp)-GEQ-(GPHyp)₅-NH₂
      DescriptionAn internally quenched fluorogenic peptide substrate that undergoes selective hydrolysis by MMP-2 and MMP-9 (kcat/Km = 14,002 s-1M-1 and 5,499 s-1M-1, respectively) at the Gly-Val bond. The peptide substrate is designed from the five triple-helical collagen sequence hydrolyzed by MMP-9. Weakly cleaved by MMP-1, MMP-3, MMP-13, and MMP-14 (kcat/Km < 600 s-1M-1). Displays suitable thermal stability and aqueous solubility. Also useful for continuously monitoring MMP triple helical peptidase (THP) activity.
      FormYellow solid
      FormulationSupplied as a trifluoroacetate salt.
      Intert gas (Yes/No) Packaged under inert gas
      Chemical formulaC₂₀₀H₂₈₃N₅₁O₆₈
      Peptide SequenceH₂N-(Gly-Pro-Hyp)₅-Gly-Pro-Lys(Mca)-Gly-Pro-Pro-Gly~Val-Val-Gly-Glu-Lys(Dnp)-Gly-Glu-Gln-(Gly-Pro-Hyp)₅-NH₂
      Purity≥95% by HPLC
      SolubilityDMSO (5 mg/ml)
      Storage 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
      ReferencesLauer-Fields, J.L., et al. 2003. J. Biol. Chem. 278, 18140.