|Other Names||Dimethylaniline monooxygenase [N-oxide-forming] 5, Dimethylaniline oxidase 5, Hepatic flavin-containing monooxygenase 5, FMO 5, FMO5|
|Target/Specificity||The synthetic peptide sequence is selected from aa 489-502 of HUMAN FMO5|
|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||In contrast with other forms of FMO it does not seem to be a drug-metabolizing enzyme.|
|Cellular Location||Microsome membrane. Endoplasmic reticulum membrane|
|Tissue Location||Expressed in fetal and adult liver.|
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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. Alternative splicing results in multiple transcript variants.
Rose, J. Phd, et al. Mol. Med. (2010) In press :
Ross, C.J., et al. Nat. Genet. 41(12):1345-1349(2009)
Wheeler, H.E., et al. PLoS Genet. 5 (10), E1000685 (2009) :
Zhang, J., et al. Drug Metab. Dispos. 34(1):19-26(2006)
Furnes, B., et al. Drug Metab. Dispos. 31(2):187-193(2003)
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