FMO3 / Unconjugated /

Product Details
Description Rabbit Polyclonal to FMO3. FMO3(Flavin-containing Monooxygenase 3) is an enzyme that in humans is encoded by the FMO3 gene. The mammalian flavin-containing monooxygenases (FMO) represent a multigene family whose gene products are localized in the endoplasmic reticulum of many tissues. The FMO3 gene contains 1 noncoding and 8 coding exons. The FMO3 gene is mapped on 1q24.3. Using quantitative RNase protection assays, FMO3 is present in low abundance in fetal liver and lung and in adult kidney and lung, and in much greater abundance in adult liver. By Western blot analysis of human liver microsomal samples ranging from 8 weeks gestation to 18 years of age, FMO1 is the major fetal isoform and FMO3 is the major adult isoform. FMO3 was expressed at intermediate levels until 11 years of age when a gender-independent increase in FMO3 expression was observed during puberty. Sufferers of trimethylaminuria may display a reduced ability to metabolize substrates for FMO3 such as nicotine. FMO3 metabolizes a number of drugs, including amphetamine, clozapine, deprenyl, metamphetamine, tamoxifen, ethionamide, thiacetazone, and sulindac sulfide.
Conjugate Unconjugated
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Target Species Rat
Applications WB
Supplier Biorbyt
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About FMO3
Flavin-containing monooxygenases (FMO) are an important class of drug-metabolizing enzymes that catalyze the NADPH-dependent oxygenation of various nitrogen-,sulfur-, and phosphorous-containing xenobiotics such as therapeutic drugs, dietary compounds, pesticides, and other foreign compounds. The human FMO gene family is composed of 5 genes and multiple pseudogenes. FMO members have distinct developmental- and tissue-specific expression patterns. The expression of this FMO3 gene, the major FMO expressed in adult liver, can vary up to 20-fold between individuals. This inter-individual variation in FMO3 expression levels is likely to have significant effects on the rate at which xenobiotics are metabolised and, therefore, is of considerable interest to the pharmaceutical industry. This transmembrane protein localizes to the endoplasmic reticulum of many tissues. Alternative splicing of this gene results in multiple transcript variants encoding different isoforms. Mutations in this gene cause the disorder trimethylaminuria (TMAu) which is characterized by the accumulation and excretion of unmetabolized trimethylamine and a distinctive body odor. In healthy individuals, trimethylamine is primarily converted to the non odorous trimethylamine N-oxide.[provided by RefSeq, Jan 2016]
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