Recombinant Human Phospho-Ubiquitin (Ser65)

Background: Ubiquitin phosphorylated at serine 65 (Ubiquitin-pSer65) is a critical signaling molecule in the PINK1–Parkin mitophagy pathway and serves as a key regulator of mitochondrial quality control. Phosphorylation at Ser65 enhances ubiquitin-mediated signaling by activating and recruiting the E3 ligase Parkin, thereby promoting the selective clearance of damaged mitochondria. pSer65-Ubiquitin is widely used in studies of mitophagy, Parkinson’s disease biology, ubiquitin signaling, kinase-substrate interactions, and drug discovery programs targeting the PINK1/Parkin pathway. This modified ubiquitin is generated through site-specific phosphorylation of ubiquitin at serine 65 using the mitochondrial kinase PINK1 under controlled in vitro conditions. The resulting phosphorylated protein provides a biologically relevant tool for investigating phosphorylation-dependent ubiquitin signaling mechanisms.