PINK1 Polyclonal Antibody

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.^3,1 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 Polyclonal Antibody can be used for immunohistochemistry (IHC) and Western blot (WB) applications. The antibody primarily recognizes full-length PINK1 at approximately 66 kDa from human, mouse, and rat samples but also detects a truncated form of the protein at approximately 33 kDa.

WARNING This product is not for human or veterinary use.

1. Trempe, J.-F., and Fon, E.A. Structure and function of parkin, PINK1, and DJ-1, the three musketeers of neuroprotection. Front. Neurol. 4, 38 (2013).

2. Sim, C.H., Gabriel, K., Mills, R.D., et al. Analysis of the regulatory and catalytic domains of PTEN-induced kinase-1 (PINK1). Hum. Mutat. 33(10), 1408-1422 (2012).

3. Barodia, S.K., Creed, R.B., and Goldberg, M.S. Parkin and PINK1 functions in oxidative stress and neurodegeneration. Brain Res. Bull. 133, 51-59 (2017).

4. Creed, R.B., and Goldberg, M.S. New developments in genetic rat models of Parkinson’s disease. Mov. Disord. 33(5), 717-729 (2018).

5. Oliveras-Salvá, M., Macchi, F., Coessens, V., et al. Alpha-synuclein-induced neurodegeneration is exacerbated in PINK1 knockout mice. Neurobiol. Aging 35(11), 2625-2636 (2014).

6. Valente, E.M., Abou-Sleiman, P.M., Caputo, V., et al. Hereditary early-onset Parkinson’s disease caused by mutations in PINK1. Science 304(5674), 1158-1160 (2004).

Kubli, D.A., Cortez, M.Q., Moyzis, A.G., et al. PINK1 is dispensable for mitochondrial recruitment of parkin and activation of mitophagy in cardiac myocytes. PLoS One 10(6), e010707 (2015).