Anti-Zebrafish Psmc4 / 26S proteasome regulatory subunit 6B

0.5mg/ml if reconstituted with 0.2ml sterile DI water. PSMC4 (Proteasome 26S Subunit, ATPase 4), also known as Rpt3, is an essential component of the 19S regulatory particle of the 26S proteasome, a multi-subunit complex responsible for ATP-dependent degradation of ubiquitinated proteins. In zebrafish (Danio rerio), Psmc4 is highly conserved and serves a critical role in maintaining cellular protein homeostasis by regulating the degradation of misfolded, damaged, or regulatory proteins.PSMC4 is one of six AAA+ ATPases (Rpt1-Rpt6) that form a hexameric ring within the base of the 19S proteasome regulatory particle. This ATPase activity is required for substrate unfolding and translocation into the 20S core particle for proteolysis. In zebrafish, psmc4 is expressed ubiquitously, with elevated expression in rapidly dividing and metabolically active tissues, underscoring its involvement in cell cycle regulation, signal transduction, and stress responses.Functional analyses in zebrafish models have demonstrated that disruption of psmc4 leads to proteasome dysfunction, accumulation of ubiquitinated proteins, and developmental abnormalities. Because of its central role in protein degradation, zebrafish PSMC4 is a valuable target for studying proteostasis, neurodegenerative disease mechanisms, and the effects of proteasome inhibitors in vivo. Protein function: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. PSMC4 belongs to the heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitinated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides. [The UniProt Consortium]