Date published: 2025-12-11

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USP14 Inhibitors

USP14 inhibitors belong to a class of chemical compounds specifically designed to target and inhibit the activity of the deubiquitinating enzyme USP14. USP14 is a proteasome-associated deubiquitinase that plays a crucial role in the ubiquitin-proteasome system, which is responsible for the selective degradation of cellular proteins. These inhibitors are designed to interfere with the catalytic function of USP14, preventing it from removing ubiquitin chains from target proteins. By inhibiting USP14, these compounds aim to modulate protein degradation processes and influence cellular homeostasis and protein quality control mechanisms. The design of USP14 inhibitors involves the identification of specific binding sites on the enzyme and the development of compounds that can interact with these sites with high affinity and selectivity. These inhibitors may come in the form of small molecules or peptides, each designed to achieve a specific mode of action in blocking USP14's catalytic activity. Research on USP14 inhibitors is ongoing, and further exploration is needed to better understand their mechanisms of action and potential applications in various biological contexts.
Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

IU1

314245-33-5sc-361215
sc-361215A
sc-361215B
10 mg
50 mg
100 mg
$138.00
$607.00
$866.00
2
(0)

IU1 functions as a selective USP14 inhibitor, characterized by its ability to modulate deubiquitination pathways. This compound engages in specific molecular interactions with the active site of USP14, leading to conformational changes that affect substrate recognition. Its unique structural features enhance binding affinity, while its reactivity profile indicates a preference for certain peptide sequences, allowing for targeted intervention in proteostasis mechanisms. The compound's stability under varying conditions further supports its role in biochemical assays.

WP1130

856243-80-6sc-364650
sc-364650A
10 mg
50 mg
$480.00
$1455.00
1
(0)

WP1130 acts as a selective inhibitor of USP14, showcasing a unique ability to disrupt ubiquitin-proteasome system dynamics. It selectively binds to the enzyme's active site, inducing conformational shifts that alter substrate affinity. This compound exhibits distinct kinetic properties, favoring specific proteolytic pathways. Its molecular architecture facilitates interactions with ubiquitin chains, influencing protein turnover and cellular homeostasis. Additionally, WP1130's robust stability enhances its utility in biochemical studies.