PON2 Human

Paraoxonase-2 Human Recombinant
Cat. No.
BT21161
Source
Escherichia Coli.
Synonyms
Serum paraoxonase, arylesterase 2, EC 3.1.1.2, EC 3.1.8.1, PON 2, Serum aryldialkylphosphatase 2, A-esterase 2, Aromatic esterase 2.
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-2 Human Recombinant is expressed in E. coli having a molecular weight of 43.5 kDa and fused to an amino terminal hexahistidine tag.
The PON2 purified by proprietary chromatographic techniques.

Product Specs

Introduction
Paraoxonase 2 (PON2) is a part of a family of genes with 65% similarity in their amino acid sequence. This protein is present in various tissues, including the pancreas. Studies show that higher levels of PON2 can decrease oxidative stress within cells and reduce their ability to oxidize LDL, suggesting its role in regulating oxidative stress.
Description
Recombinant Human Paraoxonase-2 is produced in E. coli. It has a molecular weight of 43.5 kDa and includes an amino-terminal hexahistidine tag. The PON2 protein is purified using proprietary chromatographic methods.
Physical Appearance
Clear, sterile-filtered solution.
Formulation
PON2 is supplied in a buffer solution of PBS with 50% glycerol.
Applications
Arylesterase 2 can be directly used as a positive control in various applications, such as Western blotting, ELISA, immunoprecipitation, and other immunological assays. The biological activity of this product is currently untested.
Stability
For short-term storage (1-2 weeks), keep at 4°C. For long-term storage, freeze at -20°C. Repeated freezing and thawing should be avoided.
Purity
Purity is greater than 95% as determined by SDS-PAGE, showing a single band on Western Blot analysis.
Synonyms
Serum paraoxonase, arylesterase 2, EC 3.1.1.2, EC 3.1.8.1, PON 2, Serum aryldialkylphosphatase 2, A-esterase 2, Aromatic esterase 2.
Source
Escherichia Coli.
Amino Acid Sequence
MGRLVAVGLLGIALALLGERLLALRNRLKASREVESVDLPHCHLIKGIEAGSEDID ILPNGLAFFSVGLKFPGLHSFAPDKPGGILMMDLKEEKPRARELRISRGFDLASFNP HGISTFIDNDDTVYLFVVNHPEFKNTVEIFKFEEAENSLLHLKTVKHELLPSVNDIT AVGPAHFYATNDHYFSDPFLKYLETYLNLHWANVVYYSPNEVKVVAEGFDSAN GINISPDDKYIYVADILAHEIHVLEKHTNMNLTQLKVLELDTLVDNLSIDPSSGDIW VGCHPNGQKLFVYDPNNPPSSEVLRIQNILSEKPTVTTVYANNGSVLQGSSVASVY DGKLLIGTLYHRALYCELZ.

Product Science Overview

Structure and Function

PON2 is an intracellular enzyme, unlike PON1 and PON3, which are secreted extracellularly . It has a significant role in protecting cells from oxidative stress and is involved in various physiological processes. PON2 exhibits lactonase activity, hydrolyzing lactones such as N-(3-oxododecanoyl)-L-homoserine lactone (3OC12-HSL), a quorum sensing molecule . This activity is crucial for its role in modulating bacterial infections and biofilm formation .

Role in Diseases

PON2 is associated with several diseases, including cancer, cardiovascular diseases, neurodegeneration, and diabetes . Its ability to reduce oxidative stress makes it a vital enzyme in preventing the progression of these diseases. Clinical studies have highlighted its significance as a biomarker for various conditions .

Recombinant PON2

Recombinant PON2 (rPON2) has been engineered to study its structure and function in detail. The recombinant version is often produced in E. coli and refolded from inclusion bodies to obtain an active enzyme . This allows researchers to investigate the enzyme’s catalytic properties and its interactions with other molecules. For instance, rPON2 has been shown to inhibit the biofilm formation of Pseudomonas aeruginosa more effectively than PON1 .

Post-Translational Modifications

PON2 undergoes several post-translational modifications, including glycosylation and ubiquitination . These modifications can influence its catalytic activity and stability. Understanding these modifications is crucial for developing therapeutic applications of PON2.

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