The specific activity of this product is greater than 150 pmole/min/ug. This value represents the enzyme's efficiency in hydrolyzing Ubiquitin-AMC at a pH of 8.0 and a temperature of 37°C.
UCHL1 is the smallest member of the UCH family of DUBs. It catalyzes the hydrolysis of small C-terminal adducts of ubiquitin to generate ubiquitin monomers . The protein is highly specific to neurons and cells of the diffuse neuroendocrine system and their tumors . UCHL1 is predominantly expressed in the brain, where it constitutes up to 5% of the soluble protein .
Mutations in the UCHL1 gene have been associated with several neurodegenerative disorders, including Parkinson’s disease (PD). These mutations can influence the enzyme’s catalytic activity and its tendency to aggregate . UCHL1 interacts with various proteins related to the development of PD, such as alpha-synuclein, amyloid-beta precursor protein, ubiquitin-protein ligase parkin, and heat shock proteins . The balance between UCHL1’s canonical catalytic activity and its numerous activity-independent protein-protein interactions is crucial for its role in PD .
The UCHL1 gene originated in early gnathostome evolutionary history and has been under strong purifying selection . A critical protein segment spanning amino acid residues 32 to 39 within the secretion site plays a significant role in protein stability, proper conformation, and interaction sites . This segment is crucial for understanding the pathogenesis of PD and offers a potential therapeutic target .
UCHL1 is not only a marker for neuronal injury but also has potential implications in cancer research. It is involved in regulating cell differentiation, proliferation, and transcriptional regulation . The recombinant form of UCHL1 is used in various research applications to study its role in neurodegenerative diseases and other biological processes.