The activation and execution of apoptosis, or programmed cell death, is
triggered by different proteins. The caspases (cysteinyl aspartate-specific
proteases) stand out as being crucial for this process. It is well known that
the principal caspase involved in apoptosis execution is caspase 3. Caspase 3
can be activated by diverse death-inducing signals, including chemotherapeutic
agents.
Fluofarma’s caspase 3 DAP biosensor is the most precise and sensible
technology to assess caspase 3 activity.
The understanding of caspase 3 activity and manipulation, and thus of
apoptosis can allow therapeutic intervention in major diseases such as cancer,
heart disease, stroke, AIDS, autoimmunity, degenerative diseases, and others.
Fluofarma’s proprietary caspase 3 biosensor is a chimeric construct based on a GFP-like reporter linked to a mitochondrial anchorage probe by a peptide specifically cleaved by activated caspase 3 during apoptosis. Our specific biosensor allows the assessment of caspase 3 activity as it induces relocation of the fluorescence signal from the mitochondria into the cytoplasm.
When caspase 3 is maintained inactive (by a drug compound, for example), the fluorescent biosensor remains localized to the mitochondrial outer membrane (MOM) and the cell keeps its fluorescence. In contrast, when caspase 3 is activated, the biosensor is cleaved; the GFP-like protein relocates to the cytoplasm and the fluorescence is lost after the permeabilization plasma membrane. The number of fluorescent cells in a given condition provides a quantitative measure of caspase 3 activity.