Immunohistochemistry: A reporesentative lot detected DJ-1 oxidation in various regions of murine (cerebral cortex, hippocampus, striatum, SN pars compacta, SN pars reticulata) and human (SN and red nucleus of the midbrain) brain tissue sections (Saito, Y., et al. (2014). J Neuropathol Exp Neurol. 73(7):714-728.)
Western Blotting Analysis: A reporesentative lot detected basal DJ-1 oxidation (oxDJ-1) in human neuroblastoma SH-SY5Y cells and murine fibroblasts from wild-type, but not DJ-1 knockout, mice, as well as enhanced oxDJ-1 in H2O2-treated SH-SY5Y cells (Saito, Y., et al. (2014). J Neuropathol Exp Neurol. 73(7):714-728.).
Protein DJ-1 (UniProt Q99497; also known as Parkinson disease (autosomal recessive, early onset) protein 7, Epididymis secretory sperm binding protein Li 67p, Oncogene DJ1) is encoded by the PARK7 (also known as DJ1, HEL-S-67p) gene (Gene ID 11315) in human. DJ-1 belongs to the ThiJ/PfpI family of proteins characterized by a ThiJ domain. DJ-1 is reported to be involved in multiple physiological processes, including cellular oncogenic transformation, RNA-protein interaction regulation, sperm fertilization, antioxidative defense, and transcriptional regulation. Mutations in the DJ-1 gene, PARK7, are known causes of autosomal recessive parkinsonism with a clinical presentation similar to other forms of recessive PD syndromes. DJ-1 cysteine residue 106 (Cys106) is preferentially oxidized through direct oxygen addition in response to cellular oxidative stress. Cysteine forms 3 different oxidized species, cysteine–sulfenic acid (Cys-SOH), cysteine–sulfinic acid (Cys-SO2H), and cysteine–sulfonic acid (Cys-SO3H). The Cys-SO2H form of oxDJ-1 is likely the active form, and further oxidation to Cys-SO3H leads to loss of biologic function. The levels of oxDJ-1 in erythrocytes from unmedicated PD patients are reported to be markedly higher than those from medicated PD patients and healthy subjects.
