Caspase Substrate
Caspase Substrate - Related Videos
08:16
In Vitro Cleavage Assays using Purified Recombinant Drosophila Caspases for Substrate Screening
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2022
Here we present a protocol to express and purify recombinant Drosophila caspases Dronc and Drice, and their use in in vitro cleavage assays.
02:54
Caspase-3/7 Assay: A Luminescence-Based Assay to Quantify Apoptosis by Measuring Caspase-3/7 Activities in Frog Skin Explants
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2025
This video describes an in vitro Caspase-3/7 luminescent assay to quantify cell death or apoptosis. The assay measures luminescence produced following caspase-3/7 cleavage of a pro-luminescent DEVD substrate. The luminescence generated is proportional to caspase-3/7 activity.
05:29
Measuring Caspase Activity Using a Fluorometric Assay or Flow Cytometry
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Cited by 6 •
2023
The present protocol describes two methods to measure caspase activity through a fluorogenic substrate using flow cytometry or a spectrofluorometer.
04:01
Assessment of the Activation of Multiple Caspases in Macrophages
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2025
This video demonstrates the assessment of multiple caspase activations in bone marrow-derived macrophages through stimulation with the influenza virus. Following macrophage lysis, heat-inactivation of lysate, and centrifugation, intracellular caspases are collected for subsequent immunological analysis.
05:18
Quantification of Immunostained Caspase-9 in Retinal Tissue
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Cited by 4 •
2022
Presented here is a detailed immunohistochemistry protocol to identify, validate, and target functionally relevant caspases in complex tissues.
FAQs
Caspase recognition depends on a short sequence motif that contains an essential aspartate residue. The enzyme hydrolyzes the peptide bond immediately after that residue, so cleavage is sequence-directed rather than a nonspecific breakdown of the protein. This specificity lets investigators connect a detected cleavage event to caspase activity and examine which cellular proteins may be affected.
Cleavage can alter or disable substrate function by splitting the protein or peptide at the recognized site. In neurons, that functional change can help explain how caspase activation is associated with apoptosis, axonal degeneration, or cell injury. Measuring the resulting cleavage therefore links enzymatic activity with potential changes in cellular behavior.
When a known substrate is cleaved, the event can serve as a molecular readout of caspase activity. Examining these cleavage markers helps characterize death-signaling pathways and identify cellular targets of active caspases. This approach adds molecular detail to studies of neuronal injury by showing that caspase-associated processing has occurred in the cellular system being examined.
Researchers assess cleavage of selected protein or peptide substrates and interpret the resulting cleavage marker as an indication of caspase activity. In neuroscience studies, this analysis can be applied to neuronal apoptosis, axonal degeneration, or cell injury. Comparing cleavage findings across experimental conditions can also help evaluate whether a neuroprotective intervention affects death-signaling activity.
These markers can indicate which cellular targets are affected after caspase activation. Because different substrates may undergo cleavage as caspases act, their analysis helps connect enzymatic activity with changes in protein function and with specific death-signaling pathways. In neuronal research, that information supports characterization of the molecular events accompanying apoptosis, degeneration, or injury.
They provide a molecular way to examine caspase-associated events in conditions involving neuronal damage. By analyzing substrate cleavage, investigators can characterize apoptosis and axonal degeneration, identify cellular targets of active caspases, and assess death-signaling pathways. The same measurements can support evaluation of potential neuroprotective interventions by showing whether caspase-related processing changes.