PON1 Human

Paraoxonase-1 Human Recombinant
Cat. No.
BT21005
Source
Escherichia Coli.
Synonyms
Serum paraoxonase, arylesterase 1, EC 3.1.1.2, EC 3.1.8.1, PON 1, Serum aryldialkylphosphatase 1, A-esterase 1, Aromatic esterase 1, K-45, ESA, PON.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 95% as determined by SDS-PAGE.
Single band on Western Blot.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

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.

Product Specs

Introduction
Paraoxonase 1, also known as Esterase-A, plays a crucial role in detoxifying organophosphate insecticides like parathion. It may also offer protection against coronary artery disease by breaking down proinflammatory oxidized lipids found in oxidized low-density lipoproteins (LDLs).
Description
Recombinant Human Paraoxonase-1 Isoform is produced in E. coli. It is fused to a 4.5kDa amino-terminal hexahistidine tag, resulting in a total molecular weight of 42.9kDa. The purification of PON1 is achieved using proprietary chromatographic methods.
Physical Appearance
A clear solution that has been sterilized by filtration.
Formulation
PON1 is provided in a buffer solution of 20mM Tris-HCl at a pH of 8.0 and 50% glycerol.
Stability
For short-term storage (1-2 weeks), keep at 4°C. For extended storage, freeze at -20°C. Minimize repeated freeze-thaw cycles.
Purity
Purity exceeding 95% as determined by SDS-PAGE analysis. Appears as a single band on Western Blot.
Synonyms
Serum paraoxonase, arylesterase 1, EC 3.1.1.2, EC 3.1.8.1, PON 1, Serum aryldialkylphosphatase 1, A-esterase 1, Aromatic esterase 1, K-45, ESA, PON.
Source
Escherichia Coli.
Amino Acid Sequence
MAKLIALTLLGMGLALFRNHQSSYQTRLNALREVQPVELPNCNLVKGIE
TGSEDLEILPNGLAFISSGLKYPGIKSFNPNSPGKILLMDLNEEDPTVLE
LGITGSKFDVSSFNPHGISTFTDEDNAMYLLVVNHPDAKSTVELFKFQE
EEKSLLHLKTIRHKLLPNLNDIVAVGPEHFYGTNDHYFLDPYLRSWEM
YLGLAWSYVVYYSPSEVRVVAEGFDFANGINISPDGKYVYIAELLAHKIHV
YEKHANWTLTPLKSLDFNTLVDNISVDPETGDLWVGCHPNGMKIFFYD
SENPPASEVLRIQNILTEEPKVTQVYAENGTVLQGSTVASVYKGKLLIGT
VFHKALYCELZ.

Product Science Overview

Discovery and Function

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 .

Genetic and Structural Insights

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 .

Recombinant PON1

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 .

Therapeutic Potential

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 .

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