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redcoon België GENTAUR BVBA

VAT BE0473327336

Av. de l Armee 68 B4

1040 Brussels BELGIUM

  Tel + 32 16 58 90 45 

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SIRET 48423788800017

Rue Lagrange, 9

75005 Paris, France

 Tel 01 43 25 01 50

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52074 Aachen, Germany

 Tel 0241 40 08 90 86

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Carboxyfluorescein Caspase Detection Kits ™
Apoptosis detection and in situ labeling of active caspase in live cells.
 
Key Benefits:
  • Non-cytotoxic assay arrests further apoptotic activity via caspase inhibition.
  • Cell permeablity permits direct visualization of cytosolic apoptotic events.
  • Apoptotic cell population does not diminish over time.
  • Add reagent directly to cells. No special buffer or media needed. No preparation of cell lysates required. Simple wash procedure.
  • Works in diverse cell lines: human, rodent, Drosophila.
  • Can be performed in conjunction with Annexin staining, TUNEL, antibody staining, or with other APO LOGIX reagents on the same population of cells.
  • Permits high through-put screening. Protocol can be adapted for ex vivo as well as in situ experiments.
  • Works with fluorescence microscopy, 96-well fluorescence plate readers, or flow cytometry.
  • Yields both quantitative and qualitative results. Gives strong signal with little background noise.
  • Mark activity across the range of caspase proteins. Poly-caspase and caspase-specific assays to target caspases 1, 2, 3, 6, 8, 9, or 10 are available.
  • Applications - Flow Cytometry, Fluorescence Plate Reader, Fluorescent Microscope
Assay Principle:
APO LOGIX Carboxyfluoroscein Caspase Detection Kits label active caspases in living cells undergoing apoptosis. Cell Technology’s probes utilize carboxyfluorescein(FAM)-labeled peptide fluoromethyl ketone (FMK) caspase inhibitors (FAM-peptide-FMK). These FAM-peptide-FMK compounds are both cell permeable and non-cytotoxic during the course of the assay and thus allow the detection of active caspases in living cell systems.
 
 
References:
  1. Slee, E. A., C. Adrain, and S. J. Martin. 1999. Serial Killers: ordering caspase activation events in apoptosis. Cell Death and Differ. 6:1067-1074.
  2. Walker, N. P., R. V. Talanian, K. D. Brady, L. C. Dang, N. J. Bump, C. R. Ferenz, S. Franklin, T. Ghayur, M. C. Hackett and L. D. Hammill. 1994. Crystal Structure of the Cysteine Protease Interleukin-1ß-Converting Enzyme: A (p20/p10)2 Homodimer. Cell 78:343-352.
  3. Wilson, K. P., J. F. Black, J. A. Thomson, E. E. Kim, J. P. Griffith, M. A. Navia, M. A. Murcko, S. P. Chambers, R. A. Aldape, S. A. Raybuck, and D. J. Livingston. 1994. Structure and mechanism of interleukin-1 beta converting enzyme. Nature 370: 270-275.
  4. Rotonda, J., D. W. Nicholson, K. M. Fazil, M. Gallant, Y. Gareau, M. Labelle, E. P. Peterson, D. M. Rasper, R. Ruel, J. P. Vaillancourt, N. A. Thornberry and J. W. Becker. 1996. The three-dimensional structure of apopain/CPP32, a key mediator of apoptosis. Nature Struct. Biol. 3(7): 619-625.
  5. Kumar, S. 1999. Mechanisms mediating caspase activation in cell death. Cell Death and Differ. 6: 1060-1066.
  6. Thornberry, N. A., T. A. Rano, E. P. Peterson, D. M. Rasper, T. Timkey, M. Garcia-Calvo, V. M. Houtszager, P. A. Nordstrom, S. Roy, J. P. Vaillancourt, K. T. Chapman and D. W. Nicholson. 1997. A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis. J. Biol. Chem. 272(29): 17907-17911.
  7. Amstad, P.A., G.L. Johnson, B.W. Lee and S. Dhawan. 2000. An in situ marker for the detection of activated caspases. Biotechnology Laboratory 18: 52-56.
  8. Bedner, E., P. Smolewski, P.A. Amstad and Z. Darzynkiewicz. 2000. Activation of caspases measured in situ by binding or fluorochrome-labeled inhibitors of caspases (FLICA): correlation with DNA fragmentation. Exp. Cell Research 259: 308-313.
  9. Smolewski, P., E. Bedner, L. Du, T.-C. Hsieh, J. Wu, J. D. Phelps and Z. Darzynkiewicz. 2001. Detection of caspase activation by fluorochrome-labeled inhibitors: multiparameter analysis by laser scanning cytometry. Cytometry 44: 73-82.
  10. Ekert, P. G., J. Silke and D. L. Vaux. 1999. Caspase inhibitors. Cell Death and Differ. 6:1081-1086.
  11. Carcia-Calvo, M., E. Peterson, B. Leiting, R. Ruel, D. Nicholson and N. Thornberry. 1998. Inhibition of human caspases by peptide-based and macromolecular inhibitors. J. Biol. Chem. 273: 32608-32613.
  12. Hirata, H., A. Takahashi, S. Kobayashi, S. Yonehara, H. Sawai, T. Okazaki, K. Yamamoto and M. Sasada. 1998. Caspases are activated in a branched protease cascade and control distinct downstream processes in Fas-induced apoptosis. J. Exp. Med. 187: 587-600.
Kit contents
  • Lyophilized FAM labeled peptide inhibitor
  • 10X Wash Buffer
  • 10X Fixative
  • Propidium Iodide
The following kits are available:
Product
 		 Catalog No.
 		 Size
(No. of Tests)		 Price (Eur €)
FAM-VAD-FMK Poly caspase detection kit FAM100-1 25 €145
FAM100-2
 		 100 €425
FAM-DEVD-FMK Caspase 3 detection kit
 		 FAM200-1 25 €145
FAM200-2
 		 100 €425
FAM-LETD-FMK Caspase 8 detection kit FAM300-1 25 €155
FAM300-2
 		 100 €445
FAM-LEHD-FMK Caspase 9 detection kit FAM400-1 25 €145
FAM400-2
 		 100 €425
FAM-VEID-FMK Caspase 6 detection kit FAM500-1 25 €195
FAM500-2
 		 100 €495
FAM-YVAD-FMK Caspase 1 detection kit FAM600-1 25 €155
FAM600-2
 		 100 €445
FAM-VDVAD-FMK Caspase 2 detection kit FAM700-1 25 €195
FAM700-2
 		 100 €495
FAM-AEVD-FMK Caspase 10 detection kit FAM800-1 25 €195
FAM800-2
 		 100 €495