Calpains are a family of calcium-activated cysteine proteases. They convert Ca2+
signaling by modulating biological activities of their substrates through
limited proteolysis.
Calpains are implicated in numerous calcium-regulated cellular processes
including cell motility, cell-cycle progression, cell proliferation,
apoptosis, necrosis, differentiation, membrane fusion and platelet activation.
They are also thought to be involved in numerous pathologies, such as
Parkinson’s and Alzheimer’s diseases. As such, they became significant
pharmacological targets.
Fluofarma’s DAPs Calpain biosensor is the most sensible technology to
assess compounds effects on calpains activity.
Fluofarma’s proprietary calpain biosensor is a chimeric construct based on a GFP-like reporter linked to a mitochondrial anchorage probe by a peptide specifically cleaved by activated calpain. Our specific biosensor allows the assessment of calpain activity as it induces relocation of the fluorescence signal from the mitochondria into the cytoplasm.
When calpains are maintained inactive, the fluorescent biosensor protein is located at the mitochondrial outer membrane (MOM) and its fluorescence remains in the cell after plasma membrane permeabilization. In contrast, when calpain is active, 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 calpain activity.