Date published: 2025-10-23

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cathepsin S Inhibitors

Cathepsin S inhibitors belong to a specific chemical class of compounds meticulously designed to modulate the activity of cathepsin S, a lysosomal cysteine protease. Cathepsin S is involved in the degradation of various proteins within lysosomes, playing a role in antigen processing, tissue remodeling, and immune responses. These inhibitors are thoughtfully crafted molecules engineered to interact with the cathepsin S enzyme, influencing its normal function. Through these interactions, they might impact various cellular processes associated with protein degradation, immune modulation, and cellular responses, without directly altering its active sites or its involvement in lysosomal proteolysis. The design of cathepsin S inhibitors is grounded in a comprehensive understanding of the structural and functional attributes of the cathepsin S enzyme. Typically developed using advanced chemical synthesis methods and informed by insights from biochemistry and enzymology, these inhibitors are characterized by their ability to selectively bind to cathepsin S. This selectivity enables focused modulation of cellular pathways that rely on the activity of this specific enzyme. Unraveling the intricacies of protein degradation, immune regulation, and cellular interactions often employ cathepsin S inhibitors as valuable tools. The development and utilization of cathepsin S inhibitors contribute to advancing our knowledge of the complex interplay between cellular components and proteolytic dynamics, offering insights into the fundamental molecular mechanisms that govern protein turnover and contribute to cellular responses to changes in lysosomal proteolysis.
Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Leupeptin hemisulfate

103476-89-7sc-295358
sc-295358A
sc-295358D
sc-295358E
sc-295358B
sc-295358C
5 mg
25 mg
50 mg
100 mg
500 mg
10 mg
$72.00
$145.00
$265.00
$489.00
$1399.00
$99.00
19
(3)

Leupeptin hemisulfate acts as a potent inhibitor of cathepsin S, showcasing a unique ability to form stable complexes with the enzyme. Its structural features enable specific interactions with the active site, effectively blocking substrate access. The inhibition kinetics reveal a competitive mechanism, where leupeptin's affinity for cathepsin S significantly alters the enzyme's activity profile. This interaction can modulate proteolytic pathways, influencing cellular processes and protein turnover.

E-64

66701-25-5sc-201276
sc-201276A
sc-201276B
5 mg
25 mg
250 mg
$275.00
$928.00
$1543.00
14
(0)

E-64 is a selective inhibitor of cathepsin S, characterized by its ability to form covalent bonds with the enzyme's active site. This irreversible binding alters the enzyme's conformation, leading to a significant reduction in proteolytic activity. The kinetics of E-64 demonstrate a time-dependent inhibition, which highlights its unique reactivity. Its specificity for cathepsin S allows for targeted modulation of proteolytic pathways, impacting various cellular functions.

Z-FA-FMK

197855-65-5sc-201303
sc-201303A
1 mg
5 mg
$125.00
$365.00
19
(1)

Z-Phe-Ala-FMK is a synthetic inhibitor that covalently binds to the active site cysteine of Cathepsin S.

Caspase Inhibitor, Negative Control

105637-38-5sc-364672
sc-364672A
1 mg
5 mg
$113.00
$533.00
(0)

Caspase Inhibitor, Negative Control, acts as a competitive antagonist for cathepsin S, engaging in reversible interactions with the enzyme's active site. This dynamic binding alters the enzyme's substrate affinity, effectively modulating its proteolytic function. The inhibitor's unique structural features facilitate selective engagement, influencing reaction kinetics and enabling fine-tuning of cellular signaling pathways. Its behavior underscores the complexity of protease regulation in biological systems.

Cathepsin inhibitor peptide

sc-3130
1 mg
$115.00
1
(0)

Cathepsin inhibitor peptide functions as a selective modulator of cathepsin S activity, characterized by its ability to form stable complexes with the enzyme. This interaction disrupts the enzyme's catalytic efficiency by altering the conformation of the active site, leading to a decrease in substrate turnover. The peptide's specific amino acid sequence enhances its binding affinity, allowing for precise control over proteolytic processes and influencing cellular homeostasis.

K777

233277-99-1sc-507382
10 mg
$555.00
(0)

K11777 is a peptidyl vinyl sulfone inhibitor that specifically targets Cathepsin S activity.