caspase-4 Substrates

Ac-LEHD-AFC is a potent caspase-4 substrate that exhibits remarkable specificity through its unique peptide sequence. This compound undergoes hydrolysis upon caspase-4 cleavage, leading to a fluorescent signal that allows for real-time monitoring of enzymatic activity. Its design incorporates a fluorophore that enhances detection sensitivity, while the peptide backbone ensures optimal binding to the active site. The compound's kinetics reveal a rapid turnover rate, making it an effective tool for studying caspase-4 dynamics in various cellular contexts.

Ac-YVAD-AFC serves as a selective substrate for caspase-4, characterized by its unique amino acid sequence that facilitates specific interactions with the enzyme's active site. Upon cleavage, it releases a fluorescent moiety, enabling sensitive detection of caspase-4 activity. The compound's structural design promotes efficient binding and enhances reaction kinetics, allowing for precise analysis of caspase-4's role in apoptotic pathways and cellular signaling mechanisms.

Ac-VAD-AFC is a synthetic peptide substrate tailored for caspase-4, featuring a distinctive sequence that ensures high specificity for the enzyme's active site. Its design incorporates a fluorogenic group that emits fluorescence upon cleavage, providing a sensitive readout of enzymatic activity. The compound's unique interactions with caspase-4 enhance its catalytic efficiency, making it a valuable tool for studying the dynamics of apoptotic signaling and cellular regulation.

Caspase-1 substrate exhibits a unique structural conformation that facilitates its recognition by caspase-4, promoting efficient proteolytic cleavage. This substrate is characterized by specific amino acid residues that enhance binding affinity, leading to accelerated reaction kinetics. Its interactions with the enzyme's active site are critical for understanding inflammatory pathways, as it mimics natural substrates involved in cellular signaling. The substrate's stability under various conditions further supports its role in biochemical assays.

Ac-WVAD-AMC is a synthetic peptide substrate designed to selectively engage caspase-4, showcasing a unique sequence that optimally fits the enzyme's active site. This substrate undergoes rapid hydrolysis, resulting in a fluorescent signal that allows for real-time monitoring of caspase activity. Its specificity for caspase-4 over other caspases highlights its utility in dissecting apoptotic pathways, while its robust stability under diverse experimental conditions enhances its reliability in biochemical studies.

Ac-YVAD-pNA is a synthetic peptide that serves as a substrate for caspase-4, characterized by its unique YVAD sequence, which facilitates precise binding to the enzyme's active site. Upon cleavage, it releases p-nitroaniline, producing a measurable colorimetric change. This substrate exhibits a distinct reaction kinetics profile, allowing for the detailed analysis of caspase-4 activity in various cellular contexts, making it a valuable tool for studying apoptotic mechanisms.

Z-DEVD-pNA is a synthetic peptide designed specifically for caspase-4 activity assessment. Its DEVD sequence is crucial for selective recognition by the enzyme, enabling efficient substrate cleavage. The release of p-nitroaniline upon enzymatic action results in a quantifiable colorimetric shift, facilitating kinetic studies. This substrate's unique interaction dynamics with caspase-4 provide insights into apoptotic pathways, enhancing our understanding of cellular death mechanisms.

Ac-VAD-pNA is a synthetic substrate tailored for the study of caspase-4, featuring a VAD sequence that ensures high specificity for the enzyme. Upon cleavage, it releases p-nitroaniline, which can be monitored spectrophotometrically, allowing for detailed kinetic analysis. The substrate's unique structural conformation promotes effective binding to caspase-4, revealing intricate details of its catalytic mechanism and contributing to the broader understanding of apoptotic signaling pathways.

Ac-WEAD-AMC is a specialized substrate designed for investigating caspase-4 activity. Its WEAD sequence enhances selectivity, facilitating precise interactions with the enzyme. Upon cleavage, it liberates the fluorescent AMC moiety, enabling real-time monitoring of enzymatic activity. The substrate's unique conformation and hydrophobic characteristics optimize binding affinity, providing insights into the kinetics of caspase-4 and its role in cellular apoptosis and inflammation.