Date published: 2026-5-15

1-800-457-3801

SCBT Portrait Logo
Seach Input

caspase-9 Substrates

Santa Cruz Biotechnology now offers a broad range of caspase-9 Substrates for use in various applications. Caspase-9 substrates are pivotal tools in the study of apoptosis, specifically within the intrinsic or mitochondrial pathway of programmed cell death. Caspase-9 is an initiator caspase that becomes activated in response to cellular stress signals, such as DNA damage or oxidative stress, which lead to the release of cytochrome c from the mitochondria. Once activated, caspase-9 forms part of the apoptosome complex, which then cleaves and activates downstream effector caspases like caspase-3, ultimately leading to cell death. Researchers use caspase-9 substrates to monitor the enzyme's activity and to gain deeper insights into how caspase-9 initiates and regulates the apoptotic process. These substrates are essential in experiments that seek to understand the intricate signaling networks and molecular mechanisms that control apoptosis, particularly in response to internal cellular signals. Furthermore, caspase-9 substrates are widely utilized in high-throughput screening assays to identify potential modulators or inhibitors of caspase-9 activity, providing valuable information about the regulation of cell death pathways. The ability to specifically measure caspase-9 activity using these substrates is critical for advancing research in cell biology, cancer research, and neurobiology, as it sheds light on how cells maintain homeostasis and respond to damage or stress. The use of caspase-9 substrates continues to be fundamental in exploring the roles of apoptosis in development, disease, and cellular health. View detailed information on our available caspase-9 Substrates by clicking on the product name.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Ac-LEHD-AFC

210345-03-2sc-311277
sc-311277A
5 mg
10 mg
$345.00
$682.00
1
(1)

Ac-LEHD-AFC is a synthetic peptide substrate that selectively interacts with caspase-9, showcasing unique substrate specificity. Its design incorporates a fluorogenic moiety, enabling real-time monitoring of caspase activity through fluorescence. The compound exhibits rapid hydrolysis upon caspase-9 cleavage, leading to a significant increase in fluorescence intensity. This property allows for precise kinetic analysis of caspase-9 activity, providing insights into apoptotic signaling pathways.