|Other Names||Dimethylaniline monooxygenase [N-oxide-forming] 1, Dimethylaniline oxidase 1, Fetal hepatic flavin-containing monooxygenase 1, FMO 1, FMO1|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP6994c was selected from the Center region of human FMO1. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||This protein is involved in the oxidative metabolism of a variety of xenobiotics such as drugs and pesticides. Form I catalyzes the N-oxygenation of secondary and tertiary amines.|
|Cellular Location||Microsome membrane. Endoplasmic reticulum membrane|
|Tissue Location||Expressed mainly in fetal liver, adult kidney and, to a lesser extent, the intestine|
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Provided below are standard protocols that you may find useful for product applications.
Metabolic N-oxidation of the diet-derived amino-trimethylamine (TMA) is mediated by flavin-containing monooxygenase and is subject to an inherited FMO3 polymorphism in man resulting in a small subpopulation with reduced TMA N-oxidation capacity resulting in fish odor syndrome Trimethylaminuria. Three forms of the enzyme, FMO1 found in fetal liver, FMO2 found in adult liver, and FMO3 are encoded by genes clustered in the 1q23-q25 region. Flavin-containing monooxygenases are NADPH-dependent flavoenzymes that catalyzes the oxidation of soft nucleophilic heteroatom centers in drugs, pesticides, and xenobiotics.
Hines,R.N. et.al., Expert Opin Drug Metab Toxicol 2 (1), 41-49 (2006)
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