Anti-USP28 antibody

Supplementary info

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

Activity summary

USP28 also known as Ubiquitin Specific Peptidase 28 is a deubiquitinating enzyme responsible for removing ubiquitin from protein substrates. It belongs to the cysteine protease family and has a molecular mass of approximately 120 kDa. USP28 is mainly expressed in the nucleus and cytoplasm of cells and appears in various tissues including the lung liver and gastrointestinal tract. It plays a role in regulating protein stability by counteracting ubiquitination an important process for protein degradation.

Biological function summary

This deubiquitinase regulates several cellular processes such as DNA damage response cell cycle progression and apoptosis. USP28 influences protein stability by directly associating with components of the c-MYC signaling pathway. It is known to interact with and stabilize Fbw7 which is part of the ubiquitin ligase complex thereby affecting the turnover of proteins like c-MYC and cyclin E. Through these interactions USP28 helps maintain normal levels of these important regulators for healthy cellular functions.

Pathways

The enzyme plays an important part in the DNA damage response and MAPK signaling pathways. These pathways ensure proper genomic integrity and cell proliferation. USP28 enhances the stability of the key regulatory protein c-MYC in the p53 pathway emphasizing its role in cell cycle regulation. Its interaction with other proteins like Fbw7 and c-MYC allows it to modulate the rate of cell growth and division indicating its importance in controlled cellular pathways.

Associated diseases and disorders

USP28 has connections to cancer and neurodegenerative diseases. Its interactions with c-MYC are implicated in tumorigenesis particularly in colorectal and breast cancers due to the stabilization of oncogenic proteins that promote uncontrollable cell proliferation. Additionally USP28 might contribute to neurodegenerative disorders by affecting protein aggregates commonly seen in such diseases although studies are less established in this area. The enzyme's strong connection with proteins like Fbw7 and c-MYC highlights its relevance in these disease situations making it a potential target for therapeutic intervention.