Anti-TRIM41 antibody

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

TRIM41 also known as RING finger protein 3 functions as an E3 ubiquitin ligase with a mass of approximately 55 kDa. It interacts with the ubiquitin-proteasome system to tag specific proteins for degradation by attaching ubiquitin molecules. TRIM41 co-exists in the cytoplasm and nucleus of various cell types. This protein exhibits significant expression in tissues such as the liver heart and kidney pointing to its versatile roles in cellular environments.

Biological function summary

TRIM41 contributes to regulating protein turnover and homeostasis within cells. It forms part of a ubiquitin ligase complex which actively recognizes and degrades targeted proteins. This regulation ensures the balance of proteins involved in processes such as cell cycle progression and signal transduction. The protein interacts with other cellular mechanisms to facilitate appropriate cellular responses to stress or changes in the extracellular environment.

Pathways

The role of TRIM41 extends to influencing processes such as the NF-kB signaling pathway and the IRF3 pathway. The NF-kB pathway involves inflammation and immune response while TRIM41 may also modulate the IRF3 pathway which is essential in innate antiviral defense mechanisms. Additionally TRIM41 interacts with proteins like TRAF3 and TRAF6 playing a role in downstream signaling events essential for cellular regulation and protection against pathogens.

Associated diseases and disorders

TRIM41 becomes particularly relevant in the context of cancer and inflammatory diseases. Abnormal TRIM41 function associates with the development of some cancers where altered protein degradation disrupts normal cell cycle regulation. Inflammatory disorders may also involve TRIM41 due to its role in pathways mediating immune responses. The protein connects with other proteins such as p53 in cancer and NF-kB components in inflammation highlighting its contributions to pathophysiological states.