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PTEN-induced putative kinase 1 (PINK1) is a serine/threonine protein kinase that has a role in mitochondrial function.1,2 It is comprised of an N-terminal mitochondrial targeting sequence, a transmembrane domain, a serine/threonine kinase domain, and a C-terminal region.2 PINK1 is ubiquitously expressed primarily in the brain, skeletal muscle, and heart.3 It localizes to the mitochondria where it is either rapidly degraded or, under conditions of low mitochondrial membrane potential, accumulates on the outer mitochondrial membrane, where it recruits and activates the cytosolic E3 ubiquitin ligase Parkin, which targets the mitochondria for mitophagy.1,3 Pink1 knockout in rats leads to an age-dependent loss of dopaminergic neurons in the substantia nigra, as well as deficits in motor function and mitochondrial respiration.4 In mice, Pink1 knockout does not induce a loss of dopaminergic neurons without concomitant overexpression of α-synuclein in the substantia nigra.5 Loss-of-function mutations in PINK1 are causally associated with autosomal recessive early-onset Parkinson’s disease.3,6 Cayman’s PINK1 Monoclonal Antibody (Clone 3E8) recognizes primarily the full length protein at about 66 kDa in human tissues. This antibody can be used for ELISA and Western blot applications.
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1. Structure and function of parkin, PINK1, and DJ-
2. Analysis of the regulatory and catalytic domains of PTEN-
3. Parkin and PINK1 functions in oxidative stress and neurodegeneration. Brain Res. Bull. 133, 51-59 (2017).
4. New developments in genetic rat models of Parkinson’s disease. Mov. Disord. 33(5), 717-729 (2018).
5. Alpha-
6. Hereditary early-