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P0123

Sigma-Aldrich

Anti-Paraoxonase 1 (PON1) antibody produced in rabbit

~1 mg/mL, affinity isolated antibody, buffered aqueous solution

Synonym(s):

Anti-Arylesterase, Anti-Coronary Artey Disease, Susceptibility to, Anti-Coronary Spasms, Susceptibility to, Anti-Esterase A (ESA), Anti-Organophosphate Poisoning, Sensitivity to, Anti-PON1, Anti-Parathion Poisoning, Sensitivity to

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~40 kDa

species reactivity

mouse (predicted), rat (predicted), human

concentration

~1 mg/mL

technique(s)

indirect immunofluorescence: 5-10 μg/mL using human HT-29 cells
western blot: 0.5-1 μg/mL using whole extract of human colorectal adenocarcinoma HT-29 cells

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... PON1(5444)
mouse ... Pon1(18979)
rat ... Pon1(84024)

General description

Paraoxonase-1 (PON1) is a member of serum paraoxonases family, consisting of PON1, PON2, and PON3. Human PONs map to the long arm of chromosome 7. PON1 is polymorphic in human populations, and different individuals express widely different levels of this enzyme. PON1 and PON3 are expressed in the liver and secreted into the blood where they are associated with the high-density lipoprotein (HDL) particle.

Immunogen

synthetic peptide corresponding to amino acids 298-309 of human PON1, conjugated to KLH via an N-terminal cysteine residue. The corresponding sequence differs by one amino acid in mouse and two amino acids in rat. The peptide sequence differs by one amino acid in human PON2 and two amino acids in human PON3.

Application

Anti-Paraoxonase 1 (PON1) antibody produced in rabbit has been used in immunoblotting, and immunofluorescence .

Biochem/physiol Actions

Paraoxonase-1 (PON1) protects lipids from oxidation in lipoproteins, macrophages, and erythrocytes. PON1 may confer protection against coronary artery disease by destroying proinflammatory oxidized lipids present in oxidized low-density lipoproteins (LDLs). PON1 plays a key role in the detoxification of organophosphate insecticides such as parathion, chlorpyrifos and diazinon and nerve gases such as soman and sarin.

Physical form

Solution in 0.01 M phos­phate buffered saline, pH 7.4, containing 15 mM sodium azide.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Paraoxonase (PON)-1: a brief overview on genetics, structure, polymorphisms and clinical relevance
Shunmoogam N, et al.
Vascular Health, 14(3), 137-137 (2018)
Tomas Vaisar et al.
Diabetes care, 43(1), 178-186 (2019-10-11)
A subset of people with long-standing type 1 diabetes (T1D) appears to be protected from microvascular and macrovascular complications. Previous studies have focused on improved abilities to respond to glucose and its downstream effects as protective mechanisms. It is unclear
Targeted proteomics identifies paraoxonase/arylesterase 1 (PON1) and apolipoprotein Cs as potential risk factors for hypoalphalipoproteinemia in diabetic subjects treated with fenofibrate and rosiglitazone
Ronsein GE, et al.
Molecular and Cellular Proteomics, 15(3), 1083-1093 (2016)
Improving the ex vivo stability of drug ester compounds in rat and dog serum: inhibition of the specific esterases and implications on their identity
Koitka M, et al.
Journal of Pharmaceutical and Biomedical Analysis, 51, 664-678 (2010)
Graziella E Ronsein et al.
Molecular & cellular proteomics : MCP, 15(3), 1083-1093 (2015-12-17)
Low levels of high-density lipoprotein cholesterol (HDL-C) and high triglyceride levels contribute to the excess rate of cardiovascular events seen in subjects with type 2 diabetes. Fenofibrate treatment partially reverses dyslipidemia in these subjects. However, a paradoxical marked reduction in

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