Recombinant Human TTC33 protein (His tag N-Terminus)

Supplementary information

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

TTC33 also known as Tetratricopeptide Repeat Protein 33 is a protein with a mass of approximately 37 kDa. This protein is expressed in various tissues including the brain and liver suggesting a role in multiple biological processes. TTC33 contains tetratricopeptide repeat (TPR) domains which are known for facilitating protein-protein interactions. These domains indicate that TTC33 might act as a scaffolding or regulatory protein contributing to cellular functions via interaction with other proteins.

Biological function summary

Tetratricopeptide repeat domain-containing proteins often participate in the assembly and function of multiprotein complexes. TTC33 may have involvement in protein folding and stability given its TPR domains which are commonly found in chaperone-assisted protein folding. TTC33 likely participates in complex formation guiding or stabilizing interactions among various cellular proteins. This involvement could be essential in ensuring proper protein conformation and activity particularly in complex physiological systems like the nervous system.

Pathways

Tetratricopeptide repeat concept usually fits into cellular pathways that manage protein quality control and signaling. TTC33 could play roles in pathways such as protein stabilization and stress response impacting proteins like Hsp90 a chaperone protein that is essential for the proper folding and function of many client proteins. Additionally TTC33 might interact with proteins involved in ubiquitination pathways facilitating the turnover and degradation of misfolded proteins. These associations place TTC33 in important processes that maintain cellular homeostasis.

Tetratricopeptide repeat protein alterations have links to neurodegenerative diseases and cancers. Changes in TTC33 expression or functionality might relate to conditions like Alzheimer's disease where protein misfolding and aggregation are prevalent. TTC33's interactions with proteins such as tau could influence disease progression. Furthermore TTC33 may connect with proteins involved in carcinogenesis where disruptions in protein folding and degradation contribute to tumor development. These potential links make TTC33 an interesting target for further research in both neurodegenerative and oncological contexts.