Paraoxonase-1 Isoform Human Recombinant is expressed in E. coli, fused to a 4.5kDa amino terminal hexahistidine tag, having a total molecular weight of 42.9kDa.
The PON1 purified by proprietary chromatographic techniques.
PON1 was first identified due to its ability to hydrolyze and detoxify organophosphorus compounds . This discovery highlighted its potential in protecting humans from the harmful effects of these compounds. The enzyme exhibits three main activities: lactonase, arylesterase, and paraoxonase activity . These activities contribute to its role in drug metabolism and the prevention of cardiovascular and neurodegenerative diseases .
The gene encoding PON1 is located on chromosome 7 in humans. PON1 is part of a family of enzymes that includes PON2 and PON3, which share similar amino acid sequences but differ in their functions and locations within the body . PON1 and PON3 are found in the blood system, while PON2 is primarily intracellular .
Due to the limited stability of natural human PON1, researchers have developed recombinant versions of the enzyme (rePON1) to enhance its stability, solubility, and reactivity . These engineered variants are designed for higher bacterial expression and are considered potential candidates for therapeutic applications .
Recombinant PON1 has shown promise in various therapeutic areas. It has been studied for its potential use in treating organophosphate poisoning, where it demonstrated significant advantages over conventional treatments . Additionally, rePON1 has been explored for its anti-atherogenic properties, making it a candidate for the prevention and treatment of cardiovascular diseases .