Anti-USP24 antibody [11E3]

Supplementary info

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

Activity summary

USP24 also known as Ubiquitin Specific Peptidase 24 is a deubiquitinating enzyme with a molecular mass of approximately 291 kDa. This protein plays a role in the removal of ubiquitin from specific protein substrates which regulates their degradation in the proteasome. It involves the cleavage of the ubiquitin moieties and alters the stability or activity of proteins. USP24 shows expression in several tissues with notable presence in the brain and testis. The specificity of USP24 allows it to finely adjust cellular protein turnover affecting both normal cellular function and stress responses.

Biological function summary

The regulation of protein ubiquitination/deubiquitination is fundamental in maintaining cellular homeostasis. USP24 acts within this regulatory landscape to control pathways involved in cell cycle progression and DNA damage response. It can interact with other proteins and may form complexes under certain cellular conditions affecting its activity and specificity. These complexes can further indicate how USP24’s enzymatic action coordinates larger cellular processes modulating critical phases of a cell's life cycle and response to external damage.

Pathways

Proteins like USP24 play decisive roles in the ubiquitin-proteasome pathway. This pathway is essential for controlling protein degradation ensuring that excess damaged or misfolded proteins are effectively processed. USP24 specifically interacts with and stabilizes proteins like p53 which is fundamental in DNA repair pathways. It links the ubiquitin-proteasome system to critical cellular defense mechanisms against DNA damage helping maintain genomic integrity. There is also involvement with pathways related to neuronal survival suggesting a broader functional landscape for USP24 beyond cellular maintenance.

Associated diseases and disorders

Disruptions in USP24 activity have been implicated in various neurodegenerative diseases including Alzheimer's disease. Altered deubiquitination activity may contribute to the accumulation of pathogenic proteins exacerbating neuronal damage. Furthermore USP24 has connections with cancers particularly through its stabilization of tumor suppressor proteins like p53. Aberrant regulation of USP24 could result in ineffective tumor suppression leading to unchecked cellular proliferation. The relationship of USP24 with both Alzheimer's disease and cancer shows its importance in maintaining cellular and organismal health.