MitoPT® Apoptosis Detection Kit 100tests

Product ID: M0845

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Availability: In stock


Use of the MitoPT® kit allows the easy distinction between non-apoptotic red fluorescent cells and apoptotic green fluorescent cells.

Detection of the mitochondrial permeability transition event (PT) provides an early indication of the initiation of cellular apoptosis. This process, measured by the change in the membrane potential, is due to a collapse in the electrochemical gradient across the mitochondrial membrane. Changes in the mitochondrial membrane potential lead to the insertion of proapoptotic proteins into the membrane, initiating the formation of pores which dissipate the transmembrane potential, thus releasing cytochrome c into the cytoplasm. Loss of mitochondrial membrane potential, indicative of apoptosis, can be detected by a unique fluorescent cationic dye, 5,5', 6, 6'- tetrachloro- 1,1', 3, 3'- tetraethyl- benzamidazolocarbocyanin iodide, commonly known as JC-1. Once inside a non-apoptotic cell, the lipophilic MitoPT® reagent, bearing a delocalized positive charge, enters the negatively charged mitochondria where it aggregates and fluoresces red (EX 490nm/EM 590nm). When the mitochondrial membrane potential collapses in apoptotic cells, the MitoPT® reagent no longer accumulates inside the mitochondria. Instead, it is distributed throughout the cell, assuming a monomeric form, which fluoresces green (EX 490nm/EM 527nm).

Technical Data
SKU M0845
Unit Size 1kit
Detection Method Fluorescence

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References and Citations


  • Desagher, S., Osen-Sand, A., Nichols, A., Eskes, R., Montessuit, S., Lauper, S., Maundrell, K., Antonsson, B., and Martinou, J. C. Bid-induced conformational change of Bax is responsible for mitochondrial cyto- chrome c release during apoptosis. J. Cell Biol. 144 (5): 891-901 (1999).
  • Narita, M., Shimizu, S., Ito, T., Chittenden, T., Lutz, R. J., Matsuda, H., and Tsujimoto, Y. Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria. Proc. Natl. Acad. Sci. USA 95: 14681- 14686 (1998).
  • Basanez, G., Nechushtan, A., Drozhinin, O., Chanturiya, A., Choe, E., Tutt, S., Wood, K. A., Hsu, Y. T., Zimmerberg, J., and Youle, R. J. Bax , but not Bcl- X L decreases the lifetime of planar phospholipid bilayer membranes at subnano- molar concentrations. Proc. Natl. Acad. Sci. USA 96: 5492- 5497 (1999).
  • Luo, X., Budihardio, I., Zou, H., Slaughter, C., and Wang, X. Bid, a Bcl- 2 interacting protein, mediates cytochrome c release from mito- chondria in response to activation of cell surface death receptors. Cell 94: 481- 490 (1998).
  • Antonsson, B., Montessuit, S., Lauper, S., Eskes, R., Martinou, J. C. Bax oligomerization is required for channel- forming activity in liposomes and to trigger cytochrome c release from mitochondria. Biochem J. 345: 271- 278 (2000).
  • Smiley, S. T., Reers, M., Mottola- Hartshorn, C., Lin, M., Chen, A., Smith, T. W., Steele, G. D., and Chen, L. B. Intracellular heterogeneity in mitochondrial membrane potentials revealed by a J- aggregate forming lipophilic cation JC- 1. Proc. Natl. Acad. Sci. USA 88: 3671- 3675 (1991).
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