Anti-Proteasome 20S C2/HC2 antibody

Supplementary info

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

Activity summary

The Proteasome 20S C2/HC2 also known as the proteasome subunit beta type-1 represents an important component of the proteasome complex. This protein performs proteolytic functions degrading ubiquitinated proteins into peptides. The proteasome 20S C2/HC2 has a molecular mass of approximately 23 kDa and is expressed in various tissues throughout the body including muscle and nerve tissues. It forms part of the 20S core particle of the proteasome complex and contributes to protein homeostasis.

Biological function summary

Proteasome 20S C2/HC2 plays a significant role in maintaining protein quality by participating in proteolytic degradation. It forms part of the larger 26S proteasome complex which assembles with regulatory particles for substrate recognition. This protein is essential for the breakdown and removal of oxidized or misfolded proteins thereby preventing the accumulation of potentially toxic aggregates within the cell. It ensures cellular regulation by processing proteins that control various aspects of cell cycle signaling and differentiation.

Pathways

The activity of the Proteasome 20S C2/HC2 integrates directly into the ubiquitin-proteasome pathway. This pathway regulates protein turnover and plays a vital role in cellular processes such as the cell cycle and apoptosis. The association with proteins such as ubiquitin and E3 ligases is critical for the marking of substrate proteins for degradation. This protein is also linked to the NF-kB signaling pathway interacting with proteins that modulate immune and inflammatory responses demonstrating its influence on broader regulatory networks.

Associated diseases and disorders

Proteasome 20S C2/HC2 disruption has been identified in various pathological conditions. Abnormal function or expression levels relate to neurodegenerative disorders like Parkinson’s disease where inefficient protein degradation leads to protein aggregation. This protein also connects to tumor progression in cancers where alterations in the ubiquitin-proteasome system affect cell cycle regulation and apoptosis. The protein's interaction with tumor suppressors and oncogenes highlights its significance in cellular growth abnormalities.