616407 TACE Substrate IV, Fluorogenic - Calbiochem

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616407-1MG
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      Description
      OverviewAn internally-quenched fluorogenic decapeptide substrate that is useful for continuous monitoring of TACE activity and high-throughput screening of TACE inhibitors (kcat = 21.6 s-1 and substrate concentration at half the Vmax, S0.5 = 342 µM). The substrate is cleaved at Ala-Val amide bond. Acts as a poor substrate for MMP-1, MMP-9, and MMP-13. Displays better solubility in aqueous buffers.
      Catalogue Number616407
      Brand Family Calbiochem®
      SynonymsTNF-α Convertase Enzyme Substrate IV, Fluorogenic, Abz-LAQAVRSSSR-Dpa, ADAM-17 Substrate IV, Fluorogenic
      References
      ReferencesJin, G., et al. 2002. Anal. Biochem. 302, 269.
      Product Information
      ATP CompetitiveN
      FormYellow lyophilized solid
      FormulationSupplied as a trifluoroacetate salt.
      Hill FormulaC₅₉H₉₃N₂₃O₂₀
      Chemical formulaC₅₉H₉₃N₂₃O₂₀
      ReversibleN
      Quality LevelMQ100
      Applications
      Biological Information
      Primary TargetFluorogenic decapeptide substrate that is useful for continuous monitoring of TACE activity
      Primary Target IC<sub>50</sub>kcat = 21.6 s-1 and substrate concentration at half the Vmax, S0.5 = 342 µM
      Purity≥95% by HPLC
      Physicochemical Information
      Cell permeableN
      Emission max.
      Excitation max.
      Peptide SequenceAbz-Leu-Ala-Gln-Ala-Val-Arg-Ser-Ser-Ser-Arg-Dpa
      Dimensions
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Storage and Shipping Information
      Ship Code Ambient Temperature Only
      Toxicity Standard Handling
      Storage +2°C to +8°C
      Protect from Light Protect from light
      Protect from Moisture Protect from moisture
      Do not freeze Ok to freeze
      Special InstructionsFollowing reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 6 months at -20°C.
      Packaging Information
      Transport Information
      Supplemental Information
      Specifications

      Documentation

      TACE Substrate IV, Fluorogenic - Calbiochem SDS

      Title

      Safety Data Sheet (SDS) 

      TACE Substrate IV, Fluorogenic - Calbiochem Certificates of Analysis

      TitleLot Number
      616407

      References

      Reference overview
      Jin, G., et al. 2002. Anal. Biochem. 302, 269.
      Data Sheet

      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-December-2018 JSW
      SynonymsTNF-α Convertase Enzyme Substrate IV, Fluorogenic, Abz-LAQAVRSSSR-Dpa, ADAM-17 Substrate IV, Fluorogenic
      DescriptionAn internally quenched, fluorogenic, 10-amino acid peptide substrate that is useful for monitoring TNF-α Convertase Enzyme (TACE) activity by a continuous fluorometric assay. Also useful for screening TACE inhibitors (kcat = 21.6 s-1 when the substrate concentration is half the Vmax, S0.5 = 342 µM). The substrate is cleaved at the Ala-Val amide bond. The substrate is not substantially cleaved by MMP-1, MMP-9, or MMP-13. Displays improved solubility in aqueous buffers. Excitation max: ~320 nm; Emission max: ~420 nm.
      FormYellow lyophilized solid
      FormulationSupplied as a trifluoroacetate salt.
      Recommended reaction conditions50 mM Tris-HCl, pH 7.4, 25 mM NaCl, 4% glycerol.
      Chemical formulaC₅₉H₉₃N₂₃O₂₀
      Peptide SequenceAbz-Leu-Ala-Gln-Ala-Val-Arg-Ser-Ser-Ser-Arg-Dpa
      Purity≥95% by HPLC
      SolubilityDMSO (5 mg/ml)
      Storage +2°C to +8°C
      Protect from moisture
      Protect from light
      Do Not Freeze Ok to freeze
      Special InstructionsFollowing reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 6 months at -20°C.
      Toxicity Standard Handling
      ReferencesJin, G., et al. 2002. Anal. Biochem. 302, 269.