Anti-USP11 antibody [EPR4346] - BSA and Azide free

Supplementary info

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

Activity summary

USP11 also known as ubiquitin specific peptidase 11 is a deubiquitinating enzyme with a molecular mass of approximately 110 kDa. It removes ubiquitin molecules from target proteins regulating their stability and function. This enzyme is part of the USP family and exhibits strong expression in tissues like the testes brain and thyroid. The deubiquitination process is significant in maintaining protein homeostasis by recycling ubiquitins and controlling protein degradation.

Biological function summary

Ubiquitin-specific peptidases such as USP11 participate in diverse cellular functions including DNA repair signal transduction and cell cycle progression. USP11 often operates as part of a larger regulatory complex. It modulates DNA repair by interacting with proteins involved in the repair processes such as BRCA2. Through its deubiquitination activity USP11 significantly influences cellular response to DNA damage and helps to maintain genomic stability.

Pathways

USP11 plays a role in key mechanisms like the DNA damage response and NF-kB signaling pathways. It interacts with proteins involved in these pathways offering a layer of regulation. In the DNA damage response pathway USP11 associates with BRCA2 assisting in the repair of double-stranded breaks. In the NF-kB signaling pathway its activity can affect the degradation of IkB which allows the transcription factor NF-kB to enter the nucleus and promote gene expression.

Associated diseases and disorders

Aberrations in USP11 function have been linked to cancer and neurodegenerative diseases. In cancer alterations in USP11 might contribute to tumorigenesis by affecting the DNA repair pathways especially through the BRCA2 protein interactions. Neurodegenerative diseases may also be connected to USP11 dysfunction due to its role in the degradation of proteins that accumulate in these conditions. The enzyme's interaction with various signaling proteins suggests a potential target for therapeutic interventions in these diseases.