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400025 Caspase-1 Substrate IV, Colorimetric

Caspase-1 Substrate IV, Colorimetric MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.

Synonyms: IL-1β Converting Enzyme (ICE) Colorimetric Substrate, Ac-YVAD-pNA

400025
  
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      Overview

      Replacement Information
      Description
      Overview

      This product has been discontinued.





      Colorimetric caspase-1 substrate that is similar in sequence to Caspase-1 Substrate III, Fluorogenic (Cat. No. 400020). Cleavage of pNA is monitored colorimetrically at ~405 nm (ε = 9,160 M-1cm-1). Sequence is based on the caspase-1 cleavage site of the IL-1β precursor and includes Asp116. Also a substrate for caspase-4.
      Catalogue Number400025
      Brand Family Calbiochem®
      SynonymsIL-1β Converting Enzyme (ICE) Colorimetric Substrate, Ac-YVAD-pNA
      References
      ReferencesThornberry, N.A., and Lazebnik, Y. 1998. Science 281, 1312.
      Reiter, L.A. 1994. Int. J. Pept. Protein Res. 43, 87.
      Thornberry, N.A., et al. 1994. Methods Enzymol. 244, 615.
      Thornberry, N.A., et al. 1992. Nature 356, 768.
      Product Information
      CAS number149231-66-3
      FormLyophilized
      Hill FormulaC₂₉H₃₆N₆O₁₀
      Chemical formulaC₂₉H₃₆N₆O₁₀
      Sold on the basis of peptide contentY
      Structure formula ImageStructure formula Image
      Applications
      Biological Information
      Purity≥95% by HPLC
      Physicochemical Information
      Peptide ContentY
      Peptide SequenceAc-Tyr-Val-Ala-Asp-pNA
      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 -20°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). DMSO stock solutions are stable for up to 6 months at -20°C.
      Packaging Information
      Transport Information
      Supplemental Information
      Specifications
      Global Trade Item Number
      Catalogue Number GTIN
      400025 0

      Documentation

      References

      Reference overview
      Thornberry, N.A., and Lazebnik, Y. 1998. Science 281, 1312.
      Reiter, L.A. 1994. Int. J. Pept. Protein Res. 43, 87.
      Thornberry, N.A., et al. 1994. Methods Enzymol. 244, 615.
      Thornberry, N.A., et al. 1992. Nature 356, 768.

      Brochure

      Title
      Caspases and other Apoptosis Related Tools Brochure
      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.

      Revision01-April-2011 RFH
      SynonymsIL-1β Converting Enzyme (ICE) Colorimetric Substrate, Ac-YVAD-pNA
      DescriptionInterleukin-1β converting enzyme (ICE) is a cysteine protease that cleaves the IL-1β precursor to mature IL-1β. Substrate sequence is based on the ICE cleavage site and includes Asp116. Cleavage is monitored colorimetrically at 405 nm (ε = 9160 cm-1 M-1).
      FormLyophilized
      CAS number149231-66-3
      Chemical formulaC₂₉H₃₆N₆O₁₀
      Peptide SequenceAc-Tyr-Val-Ala-Asp-pNA
      Structure formulaStructure formula
      Purity≥95% by HPLC
      SolubilityDMSO (10 mM)
      Storage Protect from moisture
      Protect from light
      -20°C
      Do Not Freeze Ok to freeze
      Special InstructionsFollowing reconstitution aliquot and freeze (-20°C). DMSO stock solutions are stable for up to 6 months at -20°C.
      Toxicity Standard Handling
      ReferencesThornberry, N.A., and Lazebnik, Y. 1998. Science 281, 1312.
      Reiter, L.A. 1994. Int. J. Pept. Protein Res. 43, 87.
      Thornberry, N.A., et al. 1994. Methods Enzymol. 244, 615.
      Thornberry, N.A., et al. 1992. Nature 356, 768.