Date published: 2025-10-27

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Cyclophilin Inhibitors

Santa Cruz Biotechnology now offers a broad range of Cyclophilin Inhibitors for use in various applications. Cyclophilins are a family of peptidyl-prolyl isomerases that play a crucial role in protein folding, trafficking, and signaling by catalyzing the cis-trans isomerization of proline residues in polypeptide chains. Cyclophilin Inhibitors are essential tools in scientific research, allowing for the investigation of cyclophilin function and its involvement in various cellular processes, including protein folding, immune response regulation, and intracellular signaling pathways. By inhibiting cyclophilin activity, researchers can explore the enzyme's role in maintaining cellular homeostasis and its impact on the regulation of protein conformation and function. These inhibitors are widely used in studies aimed at understanding the molecular mechanisms underlying protein folding diseases, the role of cyclophilins in viral replication, and their involvement in various cellular stress responses. Additionally, Cyclophilin Inhibitors are valuable in research focusing on the interaction between cyclophilins and other cellular proteins, offering insights into the complex networks that regulate protein dynamics within cells. The availability of these inhibitors has significantly advanced research in fields such as molecular biology, biochemistry, and cell biology, providing critical tools for dissecting the intricate functions of cyclophilins and their broader implications in cellular physiology. By facilitating the precise modulation of cyclophilin activity, these inhibitors serve as indispensable tools for uncovering the molecular underpinnings of protein folding and the regulation of cellular processes. View detailed information on our available Cyclophilin Inhibitors by clicking on the product name.
Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Juglone

481-39-0sc-202675
sc-202675A
1 g
5 g
$66.00
$222.00
6
(1)

Juglone, a naturally occurring naphthoquinone, demonstrates intriguing interactions with cyclophilins, particularly through its ability to form stable complexes that influence protein folding and stability. Its unique electron-rich structure facilitates π-π stacking interactions, enhancing binding affinity. This compound can modulate enzymatic activity by altering the conformational dynamics of target proteins, potentially impacting cellular signaling pathways and regulatory mechanisms.