The product of the Parkinson's disease 7 (Park7/DJ-1) gene belongs to the peptidase C56 family of proteins and appears to have two transcriptional variants. It is a positive regulator of androgen receptor-dependent transcription, and some evidence suggests it may also function as a redox-sensitive chaperone and sensor for oxidative stress. It apparently protects neurons against oxidative stress and cell death. Defects in the Park7 gene result in the autosomal recessive form of early-onset Parkinson’s disease. While much work has focused on underlying genetic factors in this disease, less is known about the specific molecular interactions. Jin, et. al. first used Park7 antibody to identify five novel proteins complexed with Park7/DJ-1 and alpha-synuclein, suggesting their role as docking proteins and clearing up some earlier controversial studies on complex formation (1).
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Western Blot: Park7(DJ-1) Antibody
Then, Usami, et. al. first used the Park7 antibody to confirm that the protein associates with membraneous organelles such as synaptic vesicles to disrupt their normal function and cause dopaminergic neuronal degeneration (2). Promising results with Park7 antibody in Lin’s lab indicate that post-translationally modified isoforms of Park7 in whole blood could serve as biomarkers of last-stage Parkinson disease (where total Park7 levels are not useful) (3). Intriguing studies looking at Park7’s role in oxidative stress include improper mitochondrial complex 1 assembly in the absence of Park7 as observed with Park7 antibody (4).Cuevas, et. al. were also able to show with the Park7 antibody that Park7 may also be involved in hypertension pathogenesis associated with the D2 dopamine receptor-dependent signaling of increased reactive oxygen species (ROS) in the kidney (5).
