PARK7 Mouse Recombinant is produced in E. coli as a single, non-glycosylated polypeptide chain containing 212 amino acids (1-189 a.a) and has a molecular mass of 22.4 kDa . The recombinant protein is fused to a 23 amino acid His-tag at the N-terminus, which facilitates its purification through chromatographic techniques .
DJ-1 exhibits several types of catalytic activity, including functioning as a protein deglycase (EC 3.5.1.124) . It acts as a positive regulator of androgen receptor-dependent transcription and may function as a redox-sensitive chaperone, sensing oxidative stress and protecting neurons against oxidative stress and cell death .
In different cellular compartments, DJ-1 exhibits both catalytic and non-catalytic functions. For instance, oxidative stress promotes the dissociation of cytoplasmic DJ-1 dimers into monomers, which are then translocated to the nucleus. In the nucleus, DJ-1 acts as a coactivator of various signaling pathways, preventing cell death . In mitochondria, DJ-1 is found in the synthasome, where it interacts with the β ATP synthase subunit .
Mutations in the DJ-1 gene (PARK7) are associated with autosomal recessive early-onset Parkinson’s disease (PD) . These mutations often result in impaired dimerization, stability, and folding of the protein, leading to its dysfunction . Downregulation of the DJ-1 gene increases the sensitivity of cells to neurotoxins, which is a characteristic feature of PD . Introduction of recombinant DJ-1 protein has been shown to attenuate the manifestation of PD pathology in experimental models .
The recombinant PARK7 protein is used in various research applications to study its role in neuroprotection and its potential therapeutic effects in PD models. It is also utilized in biochemical assays to understand its interaction with other proteins and its function under oxidative stress conditions .