Anti-PSMD13 antibody [EPR8524] - BSA and Azide free

Supplementary info

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

Activity summary

PSMD13 also known as 26S proteasome non-ATPase regulatory subunit 13 is a component of the 19S regulatory particle of the 26S proteasome. It has a molecular weight of approximately 46 kDa. Mechanically PSMD13 plays a role in the assembly and stabilization of the proteasome complex which is responsible for ATP-dependent degradation of ubiquitinated proteins. The protein is expressed in various tissues with significant presence in organs like the liver and kidney.

Biological function summary

Within the proteasome complex PSMD13 serves as a regulatory factor that assists in substrate recognition and unfolds misfolded proteins for degradation. As part of the 26S proteasome it associates with other regulatory subunits to modulate protein breakdown efficiently. This process is essential for maintaining protein homeostasis within cells allowing effective recycling of amino acids and removal of damaged or excessive proteins.

Pathways

The activity of PSMD13 is integral in the ubiquitin-proteasome pathway. This pathway is important for regulating the cellular protein quality control and turnover. PSMD13 is also involved in the NF-kB signaling pathway where it indirectly influences the activation of transcription factor NF-kB by controlling the degradation of IkB an inhibitor protein. It works with proteins like PSMD2 which cooperate in the function and efficiency of these pathways for cell regulation.

Associated diseases and disorders

Abnormalities in PSMD13 can contribute to neurodegenerative diseases such as Alzheimer’s disease. Faulty proteasome function may lead to the accumulation of abnormal proteins in neurons which is a hallmark of such disorders. Also it has a connection to cancer development where altered proteasome activity affects cell cycle regulation and survival. In these cases interactions with other proteins like PSMD1 further highlight its critical role in disease-related cellular activities.