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Tel + 32 16 58 90
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Other Countries
0032 (0)16 41 44 07 |
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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: |
-
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.
-
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.
-
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.
-
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.
-
Kumar, S. 1999. Mechanisms mediating caspase activation in cell
death. Cell Death and Differ. 6: 1060-1066.
-
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.
-
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.
-
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.
-
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.
-
Ekert, P. G., J. Silke and D. L. Vaux. 1999. Caspase inhibitors.
Cell Death and Differ. 6:1081-1086.
-
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.
-
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 |
|
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