|Catalog Number||Size||Price (USD)||Shopping Cart|
|MO22148||100 ul||$295.00||Buy Now | Add to Cart|
DJ-1, also known as Park7, is a cytoplasmic protein that belongs to the ThiJ/Pfp1/DJ1 superfamily that functions as protein chaperones, catalases, proteases and kinases. DJ-1 was originally cloned as an oncogene that cooperatively transforms cells together with H-ras. Mutations in the DJ-1 gene are associated with rare forms of autosomal recessive early-onset Parkinson's disease. DJ-1 may also function as a redox-sensitive chaperone, as a sensor for oxidative stress, and it apparently protects neurons against oxidative stress and cell death. Augmenting DJ-1 activity might provide novel approaches to treating chronic neurodegenerative illnesses such as Parkinson's disease and acute damage such as stroke
Image: HeLa cells stained with MO22148 (green), and CH22108 chicken antibody to vimentin (red) and DNA (blue). MO22148 antibody reveals strong cytoplasmic staining for DJ-1 in human cells, but does not bind to rodent cells
Image: Blot of 20 µg rat brain lysate (lane 1) and 20 µg HeLa cell lysate (lane 2) was probed with MO22148 antibody to DJ-1at 1:5,000. Notes that the strong single band running at about 21kDa corresponds to DJ-1 in HeLa cells, while DJ-1 is barely seen in rat brain lysate. This antibody binds also to bovine DJ-1 on western blots but does not recognize rat or mouse DJ-1.