Anti-TBP-1 antibody [EPR12153] - BSA and Azide free

Supplementary info

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

Activity summary

TBP-1 also called Tat-binding protein-1 is a critical player in the regulation of protein degradation. It is a component of the 19S regulatory particle of the 26S proteasome. The molecular mass of TBP-1 is approximately 56 kDa. Expression of TBP-1 is noted in various tissues reflecting its essential role in cellular processes. As a proteasome member it contributes to the recognition and unfolding of ubiquitinated proteins designated for degradation.

Biological function summary

TBP-1 functions as an ATPase in the 26S proteasome complex aiding in the breakdown of proteins. This breakdown is important for maintaining protein homeostasis by removing misfolded or damaged proteins. In the proteasome complex TBP-1 collaborates with other ATPases to control access of substrates to the proteolytic core. This role ensures a regulated protein turnover which is important for cell cycle progression and stress responses.

Pathways

TBP-1 serves a significant role in the ubiquitin-proteasome pathway and the regulation of transcription. In the ubiquitin-proteasome pathway it collaborates with other regulatory subunits to modulate proteasomal activity. TBP-1 is associated with proteins like Rpt5 and Rpt1 which are also ATPases in the 19S regulatory particle coordinating the denaturation and translocation of proteins into the 20S core particle for degradation.

Associated diseases and disorders

TBP-1's malfunction or altered expression can contribute to neurodegenerative diseases such as Parkinson's disease and Alzheimer's disease. In these conditions improper protein degradation leads to accumulation of toxic protein aggregates. Through these pathways TBP-1 interacts with proteins like alpha-synuclein in Parkinson's disease where its dysfunction exacerbates aggregation. Understanding TBP-1's role offers insights for therapeutic approaches aimed at modulating the proteasomal degradation machinery in such diseases.