Date published: 2025-10-17

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cathepsin L Substrates

Santa Cruz Biotechnology now offers a broad range of cathepsin L Substrates for use in various applications. Cathepsin L substrates are critical tools in the study of cathepsin L, a lysosomal cysteine protease that plays a vital role in intracellular protein degradation and processing. Cathepsin L is involved in various physiological processes, including antigen presentation, tissue remodeling, and the turnover of cellular components. In scientific research, cathepsin L is particularly significant due to its role in pathological conditions, such as cancer metastasis, neurodegenerative diseases, and cardiovascular disorders, where its activity is often dysregulated. Researchers use cathepsin L substrates to monitor the enzyme's activity, enabling detailed studies of how it functions within different cellular environments. These substrates are employed in assays designed to quantify cathepsin L activity, investigate its substrate specificity, and explore the mechanisms by which it contributes to disease progression. Moreover, cathepsin L substrates are utilized in high-throughput screening assays to identify potential inhibitors or modulators of the enzyme, providing insights into new strategies for managing diseases associated with cathepsin L dysregulation. The ability to accurately measure cathepsin L activity is essential for advancing our understanding of its role in both normal cellular physiology and in the pathology of various diseases. These substrates are indispensable for researchers aiming to study the complex biological processes regulated by cathepsin L. View detailed information on our available cathepsin L Substrates by clicking on the product name.

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Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Cathepsin L substrate Substrate

65147-22-0sc-3136A
sc-3136
sc-3136B
5 mg
25 mg
100 mg
$100.00
$260.00
$694.00
11
(0)

Cathepsin L substrate is characterized by its ability to undergo selective cleavage by cathepsin L, facilitated by specific interactions with the enzyme's active site. The substrate's unique peptide sequence promotes optimal binding, enhancing catalytic efficiency. Reaction kinetics reveal a rapid turnover rate, indicative of its susceptibility to proteolytic activity. Additionally, the substrate's conformational flexibility allows for dynamic interactions, influencing the enzyme's substrate specificity and overall proteolytic pathway.