PINK1 - 50 µg

PTEN-induced putative kinase protein 1 (Serine/Threonine kinase PINK1) is an important protein that saves the dysfunction of mitochondria upon application of cellular stress. When the mitochondria is depolarized, PINK stabilizes and gets accumulated. When E3 Ubiquitin Ligase Parkin (PARK2) is brought to the damaged mitochondria, it is activated by PINK1 by phosphorylation at Ser 65 which in turn interacts with ubiquitin that is also phosphorylated at Ser 65. This process is important for removing the damaged mitochondria by mitophagy (selective autophagy) by mediating activation and translocation of PARK2. Recombinant human PINK1 effectively phosphorylates recombinant Parkin, mono-Ubiquitin, and poly-Ubiquitin chains. It specifically phosphorylates both Parkin and Ubiquitin at serine 65. This recombinant protein contains an MBP tag.