Apo3HTS

$275.00$1,445.00

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Description

Key Benefits

  • Homogenous assay for active caspase 3/7.
  • Breakthrough in cell lysis buffer and preservation of caspase activity.
  • Results in a no-wash, one-step assay.
  • No need to wash out media from cell samples, just add the reagent directly to your experimental samples.
  • Easy to Use: No need to make cell lysates or run Western blots.
  • Works with suspension and adherent cells.

Additional information

Kit Size

100, 500, 1000

ASSAY PRINCIPLE

<p style=”font-weight: 500; color: #666666;”>Cell Technology’s APO 3/7 HTS Assay utilizes the quenched (z-DEVD)2-R110 peptide substrate for caspase 3/7 detection. The absorption and emission properties of the R110 dye are suppressed when attached to the z-DEVD peptide sequence. When R110 is cleaved away, by active caspase3/7, form the quenching DEVD sequence, the free dye excites at 488nm and emits at 515-530 nm. As a result of a novel and proprietary Lysis Buffer System, the APO 3/7 HTS Assay is a homogenous platform that can be utilized for high throughput fluorescence plate reader applications. The reagent is directly added to the samples thus eliminating any wash steps.</p>
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<p style=”font-weight: 500; color: #666666;”><strong style=”font-weight: bold;”>Figure.</strong> In this figure, Jurkat cells were stimulated with various concentrations of staurosporine for 3 hours, after which caspase 3/7 activity was analyzed using the APO 3/7 HTS kit.</p>

Readable Documents

Title Name
Protocol Protocol.pdf
Datasheet Datasheet.pdf
msds msds.pdf

Kit contents and storage

Part# Reagent Temperature
Part# 4004 Caspase 3/7 Reagent (z-DEVD) 2 Rodamine 110, 1 Vial -20°C
Part# 3005 Cell Lysis Buffer, 1 Bottle 2-8°C

 

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.
Alnemri, E.S. et al (1996) Cell 87:171
Trends Biochem Sci 22,388 (1997)