Date published: 2026-1-6

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caspase-8 Substrates

Santa Cruz Biotechnology now offers a broad range of caspase-8 Substrates for use in various applications. Caspase-8 substrates are essential tools in the study of apoptosis, particularly in the extrinsic pathway of programmed cell death. Caspase-8 is a crucial initiator caspase that is activated upon the binding of death ligands, such as FasL or TNF-α, to their respective death receptors on the cell surface. Once activated, caspase-8 cleaves and activates downstream effector caspases, including caspase-3 and caspase-7, leading to the execution phase of apoptosis. By using caspase-8 substrates, researchers can monitor the activation and activity of this enzyme, providing critical insights into the molecular mechanisms that govern the initiation of apoptosis. These substrates are widely employed in various experimental settings to explore how caspase-8 contributes to the regulation of cell death, particularly in response to external stress signals. Furthermore, caspase-8 substrates are invaluable in high-throughput screening assays aimed at identifying new modulators or inhibitors of caspase-8 activity, which can further elucidate the complex signaling pathways involved in apoptosis. The ability to specifically measure caspase-8 activity allows researchers to dissect the roles of this enzyme in different biological contexts, including its involvement in immune responses and tissue homeostasis. The use of caspase-8 substrates is fundamental for advancing our understanding of apoptosis, making them indispensable in research focused on cell death, signal transduction, and cellular regulation. View detailed information on our available caspase-8 Substrates by clicking on the product name.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Ac-DEVD-AFC

201608-14-2sc-311274
sc-311274A
1 mg
5 mg
$65.00
$200.00
13
(1)

Ac-DEVD-AFC is a fluorogenic substrate specifically designed for caspase-8, showcasing unique interactions that facilitate its cleavage. The substrate's structure allows for efficient binding to the active site, promoting rapid hydrolysis and fluorescence emission upon enzymatic action. Its kinetic profile reveals a high turnover rate, making it an effective probe for monitoring caspase-8 activity. The substrate's design enhances specificity, minimizing cross-reactivity with other caspases, thus ensuring accurate assessment of apoptotic processes.

Ac-DEVD-pNA

189950-66-1sc-311275
sc-311275A
sc-311275B
sc-311275C
1 mg
5 mg
25 mg
250 mg
$97.00
$286.00
$734.00
$4692.00
14
(1)

Ac-DEVD-pNA is a synthetic substrate tailored for caspase-8, characterized by its ability to undergo specific proteolytic cleavage. The p-nitroaniline moiety provides a distinct chromogenic signal upon enzymatic action, allowing for sensitive detection. Its structural configuration promotes optimal interaction with the caspase-8 active site, resulting in a defined reaction kinetics profile. This substrate exhibits minimal interference from other proteases, ensuring precise measurement of caspase-8 activity in apoptotic pathways.

Ac-IETD-AFC

211990-57-7sc-311276
sc-311276A
5 mg
10 mg
$281.00
$453.00
1
(1)

Ac-IETD-AFC is a synthetic substrate designed for caspase-8, featuring a unique fluorogenic component that emits fluorescence upon cleavage. This substrate's structure enhances binding affinity to the caspase-8 active site, facilitating rapid reaction kinetics. The specific interactions between Ac-IETD-AFC and caspase-8 allow for selective detection, minimizing cross-reactivity with other caspases. Its sensitivity to enzymatic activity makes it a powerful tool for studying apoptotic signaling pathways.

Z-DEVD-AFC

sc-296746
sc-296746A
5 mg
50 mg
$151.00
$1358.00
1
(0)

Z-DEVD-AFC is a specialized fluorogenic substrate tailored for caspase-8, characterized by its unique peptide sequence that promotes selective cleavage. The substrate's design incorporates a fluorophore that emits a distinct signal upon enzymatic action, enabling real-time monitoring of caspase-8 activity. Its structural features optimize interaction with the enzyme's active site, ensuring high specificity and efficient reaction rates, making it ideal for dissecting apoptotic mechanisms.