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Caspases

Caspases

Caspase, a family of cysteine proteases, serve as effectors in apoptosis. The ced3 gene in C.elegans was first identified to be involved in apoptosis. This gene encodes the ced-3 caspase that is similar to the interleukin-1-beta converting enzyme or ICE in mammals. In addition to apoptosis, caspases also function in the inflammatory response. Inflammatory caspases are essential in activating pro-inflammatory cytokines that recruit immune cells and block the replication of pathogens inside...

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Related Experiment Video

Updated: Sep 1, 2025

In Vivo Biosensor Tracks Non-apoptotic Caspase Activity in Drosophila

In Vivo Biosensor Tracks Non-apoptotic Caspase Activity in Drosophila

Published on: November 27, 2016

Caspase sensors based on NanoLuc.

Jie Li¹, Jin-Lan Wang¹, Chun-Yang Gan¹

¹Key Laboratory of Molecular Biology on Infectious Diseases, Ministry of Education, Chongqing Medical University, Chongqing, China.

Journal of Biotechnology

|August 13, 2022

Summary

This summary is machine-generated.

Researchers developed novel NanoLock biosensors for detecting caspase activity, offering a sensitive and convenient method for studying cell death and inflammation. These dark-to-bright sensors show high signal-to-noise ratios, outperforming commercial kits.

Keywords:

Caspase Detection Method NanoLuc Sensor

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Last Updated: Sep 1, 2025

In Vivo Biosensor Tracks Non-apoptotic Caspase Activity in Drosophila

In Vivo Biosensor Tracks Non-apoptotic Caspase Activity in Drosophila

Published on: November 27, 2016

Detecting Anastasis In Vivo by CaspaseTracker Biosensor

Detecting Anastasis In Vivo by CaspaseTracker Biosensor

Published on: February 1, 2018

Lighting Up the Pathways to Caspase Activation Using Bimolecular Fluorescence Complementation

Lighting Up the Pathways to Caspase Activation Using Bimolecular Fluorescence Complementation

Published on: March 5, 2018

Area of Science:

Biochemistry
Molecular Biology
Cell Biology

Background:

Caspases are critical cysteine proteases regulating programmed cell death and inflammation.
Luciferase-based biosensors offer advantages for genetic encoding and assay convenience in detecting caspase activity.

Purpose of the Study:

To develop a new set of highly sensitive and convenient caspase biosensors based on NanoLuc luciferase.
To evaluate the performance of these novel biosensors compared to existing methods.

Main Methods:

Construction of NanoLock biosensors utilizing a NanoLuc luciferase and a mutated quencher peptide (HiBiT-R/D).
Optimization of NanoLock sensors for dark-to-bright signal conversion.
Testing NanoLock sensors for various caspases (1, 3, 6, 7, 8, 9, 10) in HEK293 cells and in vitro.

Main Results:

Optimized NanoLock sensors exhibited high signal-to-noise ratios, with >1233-fold activation by tobacco etch virus protease and >500-fold induction for caspase 3.
NanoLock sensors demonstrated superior performance over commercial kits in terms of signal-to-noise ratio and convenience.
A stable cell line expressing NanoLock-caspase 6 was established for high-throughput screening.

Conclusions:

NanoLock biosensors provide a sensitive, convenient, and versatile tool for detecting a wide range of caspase activities.
The developed NanoLock-caspase 6 cell line offers a powerful platform for screening caspase modulators.