Date published: 2026-5-8

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Caspase Substrates

Santa Cruz Biotechnology now offers a broad range of Caspase Substrates for use in various applications. Caspase substrates are essential tools in the study of apoptosis, the process of programmed cell death that is critical for maintaining cellular homeostasis, development, and immune responses. Caspases are a family of cysteine proteases that execute apoptosis by cleaving specific substrates within the cell, leading to the orderly disassembly of cellular components. By providing well-defined caspase substrates, researchers can accurately measure the activity of different caspases, enabling detailed investigations into the specific roles these enzymes play in apoptosis and other cellular processes. These substrates are widely used in assays to monitor caspase activity in real-time, facilitating studies on how apoptotic signals are initiated, propagated, and ultimately lead to cell death. Additionally, caspase substrates are instrumental in high-throughput screening for compounds that can modulate caspase activity, thereby contributing to a deeper understanding of the molecular mechanisms governing cell death and survival. In research, these substrates are applied in various experimental models to study the pathways involved in apoptosis, helping to clarify the roles of individual caspases in different types of cells and under various conditions. The use of caspase substrates is crucial for advancing knowledge in fields ranging from developmental biology to disease research, providing insights into how cells regulate life and death decisions at the molecular level. View detailed information on our available Caspase Substrates by clicking on the product name.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Ac-LEED-AFC

sc-293513
5 mg
$390.00
(0)

Ac-LEED-AFC is a selective caspase substrate that exhibits unique fluorescence properties upon cleavage. Its design incorporates an acylated amino acid sequence, which facilitates specific interactions with caspase active sites. The compound undergoes rapid hydrolysis, leading to a significant increase in fluorescence intensity, allowing for real-time monitoring of caspase activity. This distinctive behavior makes it a valuable tool for studying apoptotic pathways and protease dynamics in various biological contexts.