产品名称
Anti-Paraoxonase 1 (PON1) 兔抗, ~1 mg/mL, affinity isolated antibody, buffered aqueous solution
biological source
rabbit
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
Quality Level
Gene Information
human ... PON1(5444)
mouse ... Pon1(18979)
rat ... Pon1(84024)
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.
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.
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.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
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存储类别
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
法规信息
常规特殊物品
此项目有
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
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)
Paraoxonase (PON)-1: a brief overview on genetics, structure, polymorphisms and clinical relevance
Shunmoogam N, et al.
Vascular Health, 14(3), 137-137 (2018)
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
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)
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