Date published: 2025-10-12

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TRIM69 Activators

TRIM69 Activators include a range of compounds that indirectly enhance the functional activity of TRIM69, primarily through modulation of protein ubiquitination and degradation pathways. Thalidomide and its derivatives, Lenalidomide and Pomalidomide, exert modulatory effects on the ubiquitin-proteasome system. This modulation potentially enhances TRIM69's role in protein ubiquitination, impacting critical processes such as immune regulation and cell proliferation. Similarly, proteasome inhibitors like MG132 and Bortezomib can influence TRIM69 function by affecting protein degradation pathways, potentially enhancing its involvement in ubiquitin-mediated processes and cellular homeostasis. These interactions underscore TRIM69's pivotal role in protein quality control and degradation mechanisms.

Additionally, natural compounds like Curcumin and Resveratrol modulate TRIM69 activity by influencing cellular signaling pathways involved in stress response and survival, potentially enhancing TRIM69's ubiquitination activity. Chloroquine, affecting lysosomal function and autophagy, and Tunicamycin, impacting N-linked glycosylation, can also influence TRIM69's function in protein degradation, enhancing its role in cellular stress responses. Epoxomicin, as a specific proteasome inhibitor, further impacts TRIM69's activity by targeting ubiquitin-dependent protein degradation. Withaferin A, known for its anti-inflammatory properties, and Prostratin, affecting protein kinase C, can indirectly influence TRIM69's function in protein ubiquitination and signaling pathways. These activators collectively facilitate the enhancement of TRIM69-mediated functions in immune response and cell regulation, highlighting the complex interplay of ubiquitination and proteostasis in which TRIM69 is intricately involved.

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