Anti-Proteasome 26S S2/PSMD2 antibody

Supplementary info

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

Activity summary

Proteasome 26S S2 also known as PSMD2 is a subunit of the 26S proteasome. It plays an important role in the degradation of ubiquitinated proteins a process essential for maintaining protein homeostasis. The molecular mass of Proteasome 26S S2 is around 102 kDa. It is expressed in various tissues including the brain heart and muscle. The protein facilitates the recognition and unfolding of substrates destined for proteolysis by the 26S proteasome an activity that is instrumental in controlling the quality and abundance of proteins within the cell.

Biological function summary

Proteasome 26S S2 is an integral part of the 26S proteasome complex a large protease complex with a 20S core particle and 19S regulatory particles. This complex is responsible for degrading most intracellular proteins and is vital for regulating numerous cellular processes such as cell cycle control DNA repair and signal transduction. PSMD2 is linked with the assembly and stabilization of the 19S regulatory particle influencing the efficiency of the proteasome in recognizing and processing polyubiquitinated proteins.

Pathways

Proteasome 26S S2 is involved in ubiquitin-proteasome pathway and cell cycle regulation. In the ubiquitin-proteasome pathway it works with ubiquitin ligases and deubiquitinating enzymes to ensure selective and timely protein turnover. It is also associated with important regulatory proteins like CDC48 VCP/P97 which are involved in the ATP-dependent unfolding of proteins before proteasomal degradation. These pathways are essential for maintaining cellular protein homeostasis and managing cell cycle transitions suggesting an important regulatory role played by Proteasome 26S S2.

Associated diseases and disorders

Proteasome 26S S2 is linked to neurodegenerative diseases and cancers. In neurodegenerative diseases such as Parkinson's disease dysfunction of the proteasome can lead to the accumulation of misfolded proteins thereby exacerbating disease progression. In cancers overexpression of Proteasome 26S S2 and other proteasomal subunits could promote the degradation of tumor suppressor proteins fueling carcinogenesis. It connects with proteins like PINK1 and PARKIN in neurodegeneration and interacts with p53 in cancer pathways indicating its critical involvement in disease mechanisms.