The Product Spotlight: "When Dying is a Good Thing - Caspase Substrates and Inhibitors"

Apoptosis, or programmed cell-death, is necessary for various vital cell-processes. A group of cysteine proteases, called caspases, are activated causing a “complex cascade of events” triggering apoptosis, typically by cleaving after an Asp residue in their substrates. However, either too little or too much cell-death is a factor in many conditions including cancer, neurodegenerative diseases, and autoimmune diseases. Not all types of cells die from certain stimuli, making induced apoptosis a possibility in the treatment of cancer.1 Many peptides used for apoptosis research revolve around the caspases. Not only are the caspases involved in cell-death, but some also have a role in inflammation. Proinflammatory caspases (table 1) are accompanied by a release of proinflammatory cytokines, interleukin-1β (IL-1β) and IL-18, and trigger a lytic form of cell death. Caspase effectors must be activated and are initiated by the caspase initiators, whereas, the caspase initiators are often autoactivated.2,3 Since cleavage of caspase substrates triggers apoptosis, it is useful to study the substrate cleavage site. Caspase substrates often have fluorescent groups in order to monitor this cleavage progress. Caspase inhibitors, on the other hand, prevent cell death by blocking the action of the caspases. Peptides International offers a wide array of caspase substrates and inhibitors and we can also prepare a custom product, tailored to your apoptosis research needs.

Table 1: Types of Caspases

Proinflammatory Caspases

Initiator Caspases

Effector Caspases

Caspase 1

Caspase 2

Caspase 3

Caspase 4

Caspase 8

Caspase 6

Caspase 5

Caspase 9

Caspase 7

Caspase 11

Caspase 10


Caspase 12




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  1. S. Elmore, Toxico Pathol. 25, 495 (2007).   
  2. J. Salgado, al., J. Peptide Sci. 8, 543 (2002).
  3. P.J. Baker & S.L. Masters, J. Biol Chem.,293(18), 7068 (2018).


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