Recombinant human His-DJ-1 protein purified from E. coli.
Parkinson’s disease (PD) is the second most common neurodegenerative disorder after Alzheimer’s disease, with a prevalence of 1–2% in population aged 65 years or older. PD is a complex, multifactorial disorder that typically manifests after the age of 50 years. The pathology involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain. α-synuclein and parkin are thought to be firmly associated with PD. The exact biological function of the DJ-1 protein is currently unknown. It may play a role in the oxidative stress response, and this function could be important in preventing the onset of PD. Defects in PARK7 are the cause of autosomal recessive early-onset Parkinson disease 7 (PARK7). The human DJ-1 protein contains 189 amino acid residues. DJ-1 may possess an active site and could also be a protease/hydrolase similar to the PfpI proteases. The DJ-1 gene has been highly conserved in evolution. The structures of the mouse and human DJ-1 genes are similar, and human and mouse DJ-1 proteins display 90% amino acid identity. Acts as a positive regulator of androgen receptor-dependent transcription. May function as a redox-sensitive chaperone and as a sensor for oxidative stress. Prevents aggregation of SNCA. Protects neurons against oxidative stress and cell death. Plays a role in fertilization. Has no proteolytic activity. Has cell-growth promoting activity and transforming activity.
anti-DJ-1 (PARK7), mAb (1D7) YIF-LF-MA0282.