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Index / BBridge / Green FLICA Caspase 1 Assay Kit--FAM-YVAD-FMK / Product Detail : 97 Green FLICA Caspase 1 Assay Kit--FAM-YVAD-FMK
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#97 Green FLICA Caspase 1 Assay Kit--FAM-YVAD-FMK

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  Price : 281   EUR
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Product name : Green FLICA Caspase 1 Assay Kit--FAM-YVAD-FMK

Catalog number : 97

Quantity: 25 rxn

Availability: Yes

Supplier name : BBridge

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Measure Caspase-1 Activity in Whole, Living Cells

Caspase 1 (ICE) 

Members of the mammalian caspase family of cysteinyl aspartate-specific proteases play distinct roles in apoptosis and inflammation. Originally identified as Interleukin -1β Converting Enzyme or ICE (1, 2), caspase 1 along with caspases 4, 5, and 12 comprise the inflammatory subfamily of caspase enzymes (3). In rodents, caspase 11 is also an inflammatory caspase (3). 

Caspase 1 has also been found to play a role in processing a wide variety of proteins, most notably several cytokines (4-6) and enzymes within the glycolytic pathway (7). The creation of the inflammasome during host responses to pathogens leads to the activation of caspase 1 (8, 9) and may induce the class of cell death known as pyroptosis. Caspase 1-mediated cleavage of the pro-inflammatory cytokine interleukin 1 beta (IL-1β) results in the biologically active form of this critical immune response regulator. Furthermore, inflammation-related disease models have illustrated a role for caspase 1 in asthma, rheumatoid arthritis, multiple sclerosis and other disorders (8, 9).

Like other caspase family members, caspase 1 is a heterodimer comprised of two subunits, 20 kDa and 10 kDa in size (10, 11). Caspase 1 is autocatalytically activated following oligomerization. Active caspase enzymes exhibit catalytic and substrate specificities comprised of short tetra-peptide amino acid sequences that must contain an aspartate in the P1 position (12 - 14). These preferred tetra-peptide sequences have been used to derive peptides that specifically compete for caspase binding (15 - 17). In addition to the distinctive aspartate cleavage site at P1, the catalytic domains of the caspases typically require four amino acids to the left of the cleavage site with P4 as the prominent specificity-determining residue (14). Most inflammatory caspases prefer a hydrophobic amino acid such as tyrosine or tryptophan in the P4 position (14). Addition of a fluoromethyl ketone (FMK) to the tetrapeptide results in an irreversible linkage and permanent inactivation of the cysteine protease enzyme (18). Furthermore, conjugation of a fluorescent moiety at the amino terminus yields a probe that allows for the detection of caspase 1 activity (19 - 21).

FLICA™ Caspase 1 Detection Mechanism
The FLICA™ reagent FAM-YVAD-FMK enters each cell and irreversibly binds to activated caspase-1. Because the FAM-YVAD-FMK FLICA reagent becomes covalently coupled to the active enzyme, it is retained within the cell, while any unbound FAM-YVAD-FMK FLICA reagent diffuses out of the cell and is washed away. The remaining green fluorescent signal is a direct measure of the active caspase 1 enzyme activity present in the cell at the time the reagent was added. Cells that contain the bound FLICA™ can be analyzed by 96-well-plate based fluorometry, fluorescence microscopy, or flow cytometry. The carboxyfluorescein (FAM) FLICA™ reagent has an optimal excitation range from 490 - 495 nm and optimal emission range from 515 - 525 nm. Cells labeled with the FLICA™ reagent may be read immediately or preserved for 24 hours using the fixative. Unfixed samples may also be analyzed with propidium iodide or Hoechst stain to detect necrosis or changes in nuclear morphology respectively.

Additional caspase probes are in development. To receive pre-release information about ICT's future caspase probes, please join our newsletter list and indicate your area of interest.

  1. Black, R.A., Kronheim, S.R., Merriam, J.E., March, C.J., and Hopp, T.P. (1989) A pre-aspartate-specific protease from human leukocytes that cleaves pro-interleukin-1 beta. J. Biol. Chem. 264:5323-26.
  2. Kostura, M.J. (1989) Identification of a monocyte specific pre-interleukin 1 beta convertase activity. PNAS USA 86:5227-31.
  3. Scott, A. M., and M. Saleh. (2007). The inflammatory caspases: guardians against infections and sepsis. Cell Death Differ. 14:23-31.
  4. Ghayur, T., (1997). Caspase-1 processes IFN-gamma-inducing factor and regulates LPS-induced IFN-gamma production. Nature 386:619-23.
  5. Schmitz, J., et al., (2005) IL-33, an interleukin-1-like cytokine that signals via the IL-1 receptor-related protein ST2 and induces T helper type 2-associated cytokines. Immunity 23:479-90.
  6. Kumar, S. et. al. (2002) Interleukin-1F7B (IL-1H4/IL-1F7) is processed by caspase-1 and mature IL1F7B binds to the IL-18 receptor but does not induce IFN-gamma production. Cytokine 18:61-71.
  7. Shao, W. et al., (2007) The caspase-1 digestome identifies the glycolysis pathway as a target during infection and septic shock. J. Biol. Chem. 282:36321-29.
  8. McIntire, C. et al, (2009) Inflammasomes in infection and inflammation. Apoptosis 14:522-35.
  9. Franchi, L. et al. (2009) The inflammasome: a caspase-1-activation platform that regulates immune responses and disease pathogenesis. Nature Immunol. 10:241-47.
  10. Thornberry, N.A., et al. (1992) A novel herterodimeric cysteine protease is required for interleukin-1 beta processing in monocytes. Nature 356:768-74.
  11. Ayala, J.M., et al. (1994) IL-1beta-converting enzyme is present in monocytic cells as an inactive 45-kDa precursor. J. Immunol. 153:2592-99.
  12. Cryns, V., and Yuan, J. (1998) Proteases to die for. Genes Dev. 12:1551-1570.
  13. Talanian, R.V., Quinlan, C., Trautz, S., Hackett, M.C., Mankovich, J.A., Banach, D., Ghayur, T., Brady, K.D., and Wong, W.W. (1997) Substrate specificities of caspase family proteases. J. Biol. Chem. 272:9677-9682.
  14. Garcia-Calvo, M., Peterson, E.P., Leiting, B., Ruel, R., Nicholson, D.W., and Thornberry, N.A. (1998) Inhibition of human caspases by peptide-based macromolecular inhibitors. J. Biol. Chem. 273:32608-32613.
  15. Degterev, A., Boyce, M., and Yuan, J. (2003) A decade of caspases. Oncogene 22:8543-8567.
  16. Nicholson, D.W. (1999) Caspase structure, proteolytic substrates, and function during apoptotic cell death. Cell Death Differ. 6:1028-1042.
  17. Thornberry, N.A., and Lazebnik, Y. (1998) Caspases: enemies within. Science 281:1312-1316.
  18. Rauber, P., Angliker, H., Walker, B., and Shaw, E. (1986) The synthesis of peptidylfluoromethanes and their properties as inhibitors of serine proteases and cysteine proteinases. Biochem. J. 239:633-640.
  19. Bedner, E., Smolewski, P., Amstas, P., and Darzynkiewicz, Z. (2000) Activation of caspases measured in situ by binding of fluorochrome-labeled inhibitors of caspases (FLICA): correlation with DNA fragmentation. Exp. Cell Res. 259:308-313.
  20. Amstad, P.A., Yu, G., Johnson, G.L., Lee, B.W., Dhawan, S., and Phelps, D.J. (2001) Detection of caspase activation in situ by fluorochrome-labeled caspase inhibitors. Biotechniques 31:608-610.
  21. Smolewski, P., Bedner, E., Du, L., Hsieh, T.C., Wu, J.M., Phelps, D.J., and Darzynkiewicz, Z. (2001) Detection of caspase activation by fluorochrome-labeled inhibitors: multiparameter analysis by laser scanning cytometry. Cytometry 44:73-82.

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