UCHL1 Protein, Mouse (His)

UCHL1 Protein is a deubiquitinase that plays a crucial role in various processes, including maintenance of synaptic function, cardiac function, inflammatory response, and osteoclastogenesis. It inhibits the ubiquitination of several proteins, such as WWTR1/TAZ, EGFR, HIF1A, and beta-site amyloid precursor protein cleaving enzyme 1/BACE1. Additionally, it recognizes and hydrolyzes the peptide bond at the C-terminal glycine of ubiquitin, which helps maintain a stable pool of monoubiquitin necessary for the ubiquitin-proteasome and autophagy-lysosome pathways. UCHL1 Protein also regulates amyloid precursor protein/APP processing by promoting BACE1 degradation, leading to reduced amyloid beta production. It is involved in the immune response by regulating the ability of MHC I molecules to reach compartments essential for generating Ag-MHC I complexes. Furthermore, UCHL1 Protein mediates the deubiquitination of the transcriptional coactivator WWTR1/TAZ, stabilizing it and inhibiting osteoclastogenesis. It also stabilizes epidermal growth factor receptor EGFR, preventing its degradation and activating downstream mediators. Moreover, UCHL1 Protein modulates oxidative activity in skeletal muscle by regulating key mitochondrial oxidative proteins. Lastly, it enhances the activity of hypoxia-inducible factor 1-alpha/HIF1A by inhibiting its degradation through abrogating its VHL E3 ligase-mediated ubiquitination.