Date published: 2026-6-3

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cathepsin H Substrates

Santa Cruz Biotechnology now offers a broad range of cathepsin H Substrates for use in various applications. Cathepsin H substrates are indispensable tools in the study of cathepsin H, a lysosomal cysteine protease that is unique in its dual enzymatic activity, functioning both as an aminopeptidase and an endopeptidase. This enzyme plays a crucial role in intracellular protein degradation, particularly in the processing of proteins within the lysosome, which is essential for maintaining cellular homeostasis and facilitating the turnover of cellular components. Researchers utilize cathepsin H substrates to monitor the activity of this enzyme in various biological contexts, helping to study its role in normal physiology and in disease states where its activity may be dysregulated, such as in cancer, neurodegenerative disorders, and inflammatory conditions. These substrates are widely used in biochemical assays designed to explore the enzymatic specificity and kinetics of cathepsin H, as well as in high-throughput screening assays aimed at identifying potential inhibitors or modulators of its activity. The ability to accurately measure cathepsin H activity using these substrates is critical for advancing our understanding of how this protease contributes to cellular functions and how its dysregulation can lead to pathological outcomes. By enabling detailed investigations into the biochemical pathways regulated by cathepsin H, these substrates are essential for research in cell biology, pathology, and enzymology. View detailed information on our available cathepsin H Substrates by clicking on the product name.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

L-Arginine 7-amido-4- methylcoumarin dihydrochloride

113712-08-6sc-281539
sc-281539A
100 mg
250 mg
$139.00
$243.00
(0)

L-Arginine 7-amido-4-methylcoumarin dihydrochloride serves as a substrate for cathepsin H, showcasing unique fluorescence properties upon enzymatic cleavage. This compound undergoes hydrolysis, leading to the release of a fluorescent product, which allows for real-time monitoring of cathepsin H activity. Its design promotes specific interactions with the enzyme, enhancing reaction kinetics and providing insights into proteolytic mechanisms within biological systems.

L-Arginine-7-amido-4-methylcoumarin hydrochloride

69304-16-1sc-215211
sc-215211A
5 mg
25 mg
$107.00
$233.00
(0)

L-Arginine-7-amido-4-methylcoumarin hydrochloride acts as a selective substrate for cathepsin H, exhibiting distinctive fluorescence changes upon enzymatic action. The compound's structure facilitates precise binding to the active site of the enzyme, optimizing catalytic efficiency. Its hydrolytic breakdown generates a highly fluorescent product, enabling detailed kinetic studies and elucidation of proteolytic pathways, thereby advancing the understanding of enzyme-substrate dynamics.

L-Arginine β-naphthylamide hydrochloride

18905-73-2sc-207793
sc-207793A
1 g
5 g
$223.00
$676.00
(0)

L-Arginine β-naphthylamide hydrochloride serves as a potent substrate for cathepsin H, characterized by its unique β-naphthylamide moiety that enhances enzyme affinity. This compound undergoes specific cleavage, leading to the release of a naphthylamine derivative, which can be monitored for real-time kinetic analysis. The interaction with cathepsin H reveals insights into substrate specificity and enzyme mechanisms, contributing to a deeper understanding of proteolytic processes.