Dabcyl-YVADAPV-EDANS | 161877-70-9

Dabcyl-YVADAPV-EDANS is a synthetic peptide substrate designed for the detection and quantification of caspase-1 activity. This innovative molecule comprises a sequence that includes the specific recognition site for caspase-1, allowing for precise enzymatic cleavage. The substrate is fluorogenic, meaning it can produce a fluorescent signal upon interaction with caspase-1. The Dabcyl group acts as a quencher, while EDANS is the fluorescent donor. In its intact form, the substrate remains non-fluorescent because the energy transfer between EDANS and Dabcyl quenches fluorescence. However, once cleaved by caspase-1, the EDANS moiety is released, resulting in fluorescence that can be quantitatively measured.

One key application of Dabcyl-YVADAPV-EDANS is in biochemical assays for caspase-1 activity, particularly in research focused on inflammatory diseases where caspase-1 plays a critical role. By providing a measurable fluorescence signal, researchers can quantify the enzyme’s activity in various samples, including cell lysates and tissue extracts. This quantification is crucial for understanding the pathophysiological processes in conditions like autoinflammatory disorders, where caspase-1 is often upregulated.

Another important application lies in drug discovery and development. Dabcyl-YVADAPV-EDANS can be used to screen for potential inhibitors of caspase-1, which are of significant interest in treating diseases that involve excessive inflammation, such as sepsis or rheumatoid arthritis. By evaluating the reduction in fluorescence, researchers can identify compounds that effectively inhibit caspase-1 activity, providing leads for new therapeutic agents.

Furthermore, Dabcyl-YVADAPV-EDANS is utilized in cellular studies to monitor the induction of pyroptosis, a form of programmed cell death mediated by caspase-1. This application is vital for understanding inflammatory responses and cell death pathways. By assessing the fluorescence in live cells, scientists can determine the timing and extent of caspase-1 activation, thereby gaining insights into cellular mechanisms underpinning inflammation and immunity.

Lastly, the substrate is also employed in educational and experimental settings to demonstrate enzyme kinetics and the principles of fluorescence quenching and activation. By using this substrate in laboratory exercises, students and researchers can visually and quantitatively understand the dynamics of enzyme-substrate interactions, enhancing their comprehension of enzymatic regulation and its implications in cellular function.