Anti-TPP1 antibody [EPR16537]

Supplementary info

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

Activity summary

Tripeptidyl peptidase I (TPP1) also known as CLN2 is a lysosomal serine protease with a molecular mass of about 61 kDa. TPP1 is expressed in numerous tissues with notable activity in the brain and retinal cells. Mechanically TPP1's primary function includes cleaving N-terminal tripeptides from substrates an important step in protein degradation and turnover within the lysosome.

Biological function summary

This protease plays an essential role in maintaining cellular function by preventing the accumulation of partially degraded proteins. TPP1 exists as part of a lysosomal enzyme complex involved in the catabolic process that recycles cellular components. Its action ensures proper protein homeostasis protecting cells from toxic buildup that can lead to cellular dysfunction.

Pathways

TPP1 is a part of the lysosomal degradation pathway critical for cellular waste management and nutrient recycling. This pathway intersects with broader metabolic routes where TPP1 activity supports the catabolism of intracytoplasmic substrates. TPP1 also interacts with proteins such as cathepsin D another enzyme contributing to proteolytic pathways to maintain the balance and efficiency of protein degradation processes.

Associated diseases and disorders

TPP1 mutations are associated with neuronal ceroid lipofuscinosis type 2 (CLN2 disease) a rare neurodegenerative disorder. This disease involves progressive brain and retinal degeneration due to lysosomal storage malfunction. The TPP1 connection to CLN2 disease highlights its essential role in neurological health. Additionally TPP1 has links to Batten disease where compromised enzyme function leads to severe neurological symptoms. Other proteins like CLN3 may also interact with TPP1 in these disease contexts influencing their progression and pathology.