Paraoxonase 1 (PON1) is involved in the detoxification of several organophosphorous insecticides, including parathion, diazinon, and chlorpyrifos, as well as nerve agents, such as sarin and soman.  It also hydrolyzes aromatic esters, aromatic and aliphatic lactones, and catalyzes the hydrolysis of lipid peroxides in LDL and HDL.

 

Human PON1 is synthesized in the liver and secreted into blood, where it is bound to HDL and is proposed to be part of the plasma antioxidant system.  It is reported to be associated with protective properties towards cardiovascular disease.  Decreased PON1 activity has been associated with atherosclerosis in people with diabetes mellitus, polycystic ovary disease, familial hypercholesterolemia and renal disease.  Polymorphisms in the PON1 gene are associated with the risk of coronary artery disease, diabetic retinopathy, and age-related macular degeneration.  PON1 gene expression is induced by resveratrol, a polyphenolic phytoalexin that is thought to display cardioprotective effects.  PON1 activity has been proposed as a biomarker for liver impairment and susceptibility to organophosphate toxicity. 

 

Randox recombinant human PON1 is suitable for use by researchers from academic and government research institutions, biotechnology, diagnostic and pharmaceutical companies, as well as hospitals and reference laboratories in a wide range of research and development applications.  Potential applications include antibody production and characterisation, immunoassay development and use as a positive control or standard in immunochemical methods, including ELISA and Western blot.  Randox recombinant human PON1 is expressed both in E. coli with an amino-terminal hexahistidine tag and in CHO-K1 cells with a carboxy-terminal hexahistidine tag.