Anti-Proteasome 19S S5A/ASF antibody [EPR8936]

Supplementary info

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

Activity summary

The Proteasome 19S S5A also known as ASF or AH1 is a critical component of the proteasome complex. It is a regulatory particle of the 19S proteasome responsible for recognizing and binding polyubiquitin chains during protein degradation. This protein weighs approximately 48 kDa and is predominantly expressed in the cytoplasm and nucleus of eukaryotic cells. Its primary function is to facilitate the opening of the 20S core particle allowing for substrate entry into the proteasome for subsequent degradation.

Biological function summary

The 19S S5A operates as part of a larger proteasome complex involved in maintaining protein homeostasis. It ensures efficient degradation of ubiquitinated proteins by the 26S proteasome system playing a role in cell cycle regulation signal transduction and stress responses. The S5A subunit specifically binds ubiquitin regulating the availability of substrates subject to proteolysis which is critical for the timely removal of damaged or misfolded proteins and the regulation of various intracellular processes.

Pathways

The 19S S5A participates in the ubiquitin-proteasome pathway which is critical for protein turnover and quality control in cells. It interacts with proteins such as E3 ubiquitin ligases which tag substrates with ubiquitin chains for degradation. This process is also a part of the NF-kB signaling pathway where the proteasome degrades IκB proteins leading to the activation of NF-kB and modulation of immune responses.

Associated diseases and disorders

The 19S S5A subunit has been implicated in several pathological conditions including cancer and neurodegenerative diseases. Dysregulation of the ubiquitin-proteasome system in which 19S S5A plays a role can lead to the accumulation of damaged or misfolded proteins contributing to disorders like Parkinson's and Alzheimer's disease. Abnormal activity of associated proteins such as ubiquitin ligases and other proteasome subunits often correlates with the progression of malignancies and neurodegenerative processes.