Anti-UCH37 antibody

Supplementary info

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

Activity summary

UCH37 also known as ubiquitin carboxyl-terminal hydrolase L5 (UCHL5) is a deubiquitinating enzyme of approximately 37 kDa mass. This protein functions by cleaving ubiquitin moieties from polyubiquitin chains facilitating protein degradation or recycling processes. UCH37 expression is observed in various tissues with higher expression noted in the liver and kidney indicating its significant cellular roles in these organs.

Biological function summary

UCH37 plays a role in the ubiquitin-proteasome system where it is an integral component of the 19S regulatory particle of the 26S proteasome complex. Through this association UCH37 participates in the removal of ubiquitin from substrates targeted for proteasomal degradation. This action regulates protein turnover and prevents unnecessary degradation of proteins which is important for maintaining cell homeostasis and controlling protein quality.

Pathways

The modulation of proteostasis by UCH37 directly influences the ubiquitin-proteasome pathway and the associated cellular stress responses. Its activity can impact the NF-kappaB signaling pathway by regulating the stability of components within this pathway interacting with other proteins such as the proteasome subunit RPN13 and proteasome-associated DUBs. The precise regulation of protein levels within these pathways ensures that cells respond appropriately to stress and inflammation.

Associated diseases and disorders

Abnormal regulation or expression of UCH37 contributes to several pathological conditions. Cancer and neurodegenerative disorders are two prominent examples in which UCH37 plays a role. Elevated levels or dysfunctional UCH37 activity can disrupt proteostasis leading to uncontrolled cell proliferation or cell death resistance in cancer or the accumulation of misfolded proteins in conditions like Alzheimer’s disease. Additionally interactions of UCH37 with oncogenic proteins or tau proteins in neurodegenerative conditions reflect its relevance in the progression of these diseases.