Millipore Sigma Vibrant Logo

400011 Caspase-1 Inhibitor I, Cell-Permeable - Calbiochem

Overview

Replacement Information

Key Spec Table

Empirical Formula
C₉₇H₁₆₀N₂₀O₂₄

Pricing & Availability

Catalogue Number AvailabilityPackaging Qty/Pack Price Quantity
400011-1MGCN
Retrieving availability...
Limited Availability
Limited Availability
In Stock 
Discontinued
Limited Quantities Available
Availability to be confirmed
    Remaining : Will advise
      Remaining : Will advise
      Will advise
      Contact Customer Service
      Contact Customer Service

      Plastic ampoule 1 mg
      Retrieving price...
      Price could not be retrieved
      Minimum Quantity is a multiple of
      Maximum Quantity is
      Upon Order Completion More Information
      You Saved ()
       
      Request Pricing
      Description
      OverviewA cell-permeable inhibitor of caspase-1 (ICE; Interleukin-1β Converting Enzyme), caspase-4, and caspase-5. The C-terminal YVAD-CHO sequence of this peptide is a highly specific, potent, and reversible inhibitor of caspase-1 (Ki = 1 nM). The N-terminal sequence (amino acid residues 1-16) corresponds to the hydrophobic region (h-region) of the signal peptide of the Kaposi fibroblast growth factor (K-FGF) and confers cell-permeability to the peptide.
      Catalogue Number400011
      Brand Family Calbiochem®
      SynonymsICE Inhibitor I, Cell-permeable, YVAD-CHO, Cell-permeable, Ac-AAVALLPAVLLALLAPYVAD-CHO
      References
      ReferencesGarcia-Calvo, M., et al. 1998. J. Biol. Chem. 273, 32608.
      Hilbi, H., et al. 1998. J. Biol. Chem. 273, 32895.
      Thornberry, N.A., and Lazebnik, Y. 1998. Science 281, 1312.
      Lin, Y.-Z., et al. 1996. J. Biol. Chem. 271, 5305.
      Lin, Y.-Z., et al. 1995. J. Biol. Chem. 270, 14255.
      Reiter, L.A. 1994. Int. J. Pept. Protein Res. 43, 87.
      Thornberry, N.A., et al. 1994. Biochemistry 33, 3934.
      Thornberry, N.A., et al. 1994. Methods Enzymol. 244, 615.
      Thornberry, N.A., et al. 1992. Nature 356, 768.
      Product Information
      ATP CompetitiveN
      FormWhite solid
      Hill FormulaC₉₇H₁₆₀N₂₀O₂₄
      Chemical formulaC₉₇H₁₆₀N₂₀O₂₄
      ReversibleY
      Quality LevelMQ100
      Applications
      ApplicationCaspase-1 Inhibitor I, Cell-Permeable, inhibits the activity of caspase-1 (Ki = 1 nM), 4 & 5. The N-terminal corresponds to the h-region of the signal peptide of K-FGF that confers cell-permeability.
      Biological Information
      Primary TargetCaspase-1
      Primary Target K<sub>i</sub>1 nM
      Purity≥97% by HPLC
      Physicochemical Information
      Cell permeableY
      Peptide SequenceAc-Ala-Ala-Val-Ala-Leu-Leu-Pro-Ala-Val-Leu-Leu-Ala-Leu-Leu-Ala-Pro-Tyr-Val-Ala-Asp-CHO
      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
      Do not freeze Ok to freeze
      Special InstructionsFollowing reconstitution aliquot and freeze (-20°C). Stock solutions are stable for up to 1 month at -20°C.
      Packaging Information
      Transport Information
      Supplemental Information
      Specifications
      Global Trade Item Number
      Catalogue Number GTIN
      400011-1MGCN 04055977212624

      Documentation

      Caspase-1 Inhibitor I, Cell-Permeable - Calbiochem SDS

      Title

      Safety Data Sheet (SDS) 

      Caspase-1 Inhibitor I, Cell-Permeable - Calbiochem Certificates of Analysis

      TitleLot Number
      400011

      References

      Reference overview
      Garcia-Calvo, M., et al. 1998. J. Biol. Chem. 273, 32608.
      Hilbi, H., et al. 1998. J. Biol. Chem. 273, 32895.
      Thornberry, N.A., and Lazebnik, Y. 1998. Science 281, 1312.
      Lin, Y.-Z., et al. 1996. J. Biol. Chem. 271, 5305.
      Lin, Y.-Z., et al. 1995. J. Biol. Chem. 270, 14255.
      Reiter, L.A. 1994. Int. J. Pept. Protein Res. 43, 87.
      Thornberry, N.A., et al. 1994. Biochemistry 33, 3934.
      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.

      Revision17-July-2014 JSW
      SynonymsICE Inhibitor I, Cell-permeable, YVAD-CHO, Cell-permeable, Ac-AAVALLPAVLLALLAPYVAD-CHO
      DescriptionA cell-permeable inhibitor of caspase-1 (ICE; interleukin-1β converting enzyme). The C-terminal YVAD-CHO sequence of this peptide is a highly specific, potent, and reversible inhibitor of caspase-1 (Ki = 1 nM). The N-terminal sequence (residues 1-16) corresponds to the hydrophobic region (h-region) of the signal peptide of Kaposi fibroblast growth factor (K-FGF) and confers cell-permeability to the peptide.
      FormWhite solid
      Chemical formulaC₉₇H₁₆₀N₂₀O₂₄
      Peptide SequenceAc-Ala-Ala-Val-Ala-Leu-Leu-Pro-Ala-Val-Leu-Leu-Ala-Leu-Leu-Ala-Pro-Tyr-Val-Ala-Asp-CHO
      Purity≥97% by HPLC
      SolubilityDMSO (5 mg/ml)
      Storage -20°C
      Do Not Freeze Ok to freeze
      Special InstructionsFollowing reconstitution aliquot and freeze (-20°C). Stock solutions are stable for up to 1 month at -20°C.
      Toxicity Standard Handling
      ReferencesGarcia-Calvo, M., et al. 1998. J. Biol. Chem. 273, 32608.
      Hilbi, H., et al. 1998. J. Biol. Chem. 273, 32895.
      Thornberry, N.A., and Lazebnik, Y. 1998. Science 281, 1312.
      Lin, Y.-Z., et al. 1996. J. Biol. Chem. 271, 5305.
      Lin, Y.-Z., et al. 1995. J. Biol. Chem. 270, 14255.
      Reiter, L.A. 1994. Int. J. Pept. Protein Res. 43, 87.
      Thornberry, N.A., et al. 1994. Biochemistry 33, 3934.
      Thornberry, N.A., et al. 1994. Methods Enzymol. 244, 615.
      Thornberry, N.A., et al. 1992. Nature 356, 768.