Zebrafish Psmd13 Antibody / 26S proteasome non-ATPase regulatory subunit 13, 100 ug

Psmd13 (Proteasome 26S subunit, non-ATPase 13) is a key component of the 26S proteasome complex, which is responsible for the ATP-dependent degradation of ubiquitinated proteins. It is part of the 19S regulatory particle, which controls the recognition, unfolding, and translocation of substrates into the 20S catalytic core for degradation. Psmd13 plays an essential role in the regulation of the proteasomal function and is involved in maintaining cellular homeostasis by controlling the turnover of a wide variety of regulatory and signaling proteins.

In zebrafish, Psmd13 is the ortholog of the human PSMD13 gene, sharing high sequence identity and functional conservation between the two species. The zebrafish protein has similar domains responsible for interacting with other proteasomal components and regulatory factors, ensuring proper proteasome assembly and activity.

Like its human counterpart, Psmd13 in zebrafish may have isoforms, likely arising from alternative splicing events. These isoforms may play specialized roles in different tissues or developmental stages, potentially influencing the efficiency of protein degradation in various cellular contexts. Such isoforms could also have tissue-specific expression patterns, contributing to the regulation of cell-cycle progression, stress responses, and signal transduction.

In zebrafish, Psmd13 is highly expressed in tissues with active cell division, such as the brain, liver, and kidney, where proteasomal activity is essential for maintaining protein turnover and cellular integrity. This expression pattern aligns with the protein’s conserved role in protein quality control, cellular differentiation, and apoptosis regulation.

The study of Psmd13 in zebrafish offers valuable insights into proteasome-related diseases in humans, such as neurodegenerative diseases and cancers, where disruptions in proteasomal degradation pathways can lead to the accumulation of damaged proteins. Zebrafish serves as an excellent model for studying the molecular mechanisms of proteasomal dysfunction and for screening potential therapeutic agents aimed at modulating proteasome activity.