Anti-Phospho-Ubiquitin Ser65 (30H3K1) Recombinant Chicken Chimeric mAb

Ubiquitin phosphorylation at ser65 (pS65-Ub) is implicated in mitochondrial quality control and the molecular origins of Parkinson’s Disease. The protein kinase PINK1 phosphorylates ubiquitin at the ser65 residue in response to mitochondrial stress. This acts as a powerful "on-switch" for the E3 ubiquitin ligase Parkin increasing its enzymatic activity and recruiting it to damaged mitochondria, initiating a specialized degradation process known as mitophagy. When mitochondria are depolarized or damaged, the accumulation of pS65-Ub triggers the clearance of these damaged organelles before they can release toxic reactive oxygen species (ROS) or pro-apoptotic factors. Genetic mutations in either PINK1 or Parkin that disrupt this phosphorylation event are a primary cause of autosomal recessive juvenile Parkinsonism.

Cell Signaling / Catecholamine Signaling / Ubiquitin Signaling / Mitochondrial Biology / Neurodegenerative Disease / Alzheimer's Disease / Parkinson's Disease

Aliquot and store at ≤ -20°C for long term storage. For short term storage, store at 2-8°C. For maximum recovery of product, centrifuge the vial prior to removing the cap.

This recombinant antibody is a chimeric antibody created by replacing the mouse heavy and light constant regions of clone 30H3K1 with chicken IgY heavy and light constant regions. As such this antibody retains the same binding performance as the original clone 30H3K1 but can be detected using standard anti-chicken secondary antibodies allowing flexibility for multiplexing applications. This antibody is expressed recombinantly in mammalian cells and then affinity purified from the cell culture media.

Each new lot of antibody is quality control tested by Western blot on mock- and CCCP-treated HeLa lysates and confirmed to stain multiple bands only in CCCP treated lysates