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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. Additionally we are shipping FMO3 Proteins (6) and FMO3 Kits (1) and many more products for this protein.
Showing 10 out of 75 products:
Cow (Bovine) Polyclonal FMO3 Primary Antibody for WB - ABIN2781862
Ganti, Skapek, Zhang, Fuller, Wu, Billups, Breitfeld, Dalton, Meyer, Khoury: Expression and genomic status of EGFR and ErbB-2 in alveolar and embryonal rhabdomyosarcoma. in Modern pathology : an official journal of the United States and Canadian Academy of Pathology, Inc 2006
Show all 2 references for ABIN2781862
Human Polyclonal FMO3 Primary Antibody for EIA, WB - ABIN453026
Allerston, Vetti, Houge, Phillips, Shephard: A novel mutation in the flavin-containing monooxygenase 3 gene (FMO3) of a Norwegian family causes trimethylaminuria. in Molecular genetics and metabolism 2009
Oxidative stress-responsive transcription factor NRF2 (show GABPA Antibodies) is not indispensable for the human hepatic Flavin-containing monooxygenase-3 (FMO3) gene expression in HepG2 cells
FMO3 gene polymorphism E158K is a significant predictor of predisposition to chronic heart disease in women.
FMO3 is centrally involved in the pathogenesis of atherosclerosis by regulating cholesterol metabolism and insulin (show INS Antibodies) resistance. [Review]
FMO3 expression is increased in ob (show INS Antibodies)ese/insulin resistant patients.
These results suggest that genetic polymorphism in the human FMO3 gene may lead to changes of drug interactions for N- or S-oxygenations of xenobiotics and endogenous substances.
Effect of two-linked mutations of the FMO3 gene on itopride metabolism in Chinese healthy volunteers
Three polymorphisms were found in intronic regions of FMO3 in a child with trimethylaminuria and in her parents and a brother. The parents and brother showed no symptoms.
Comparisons of genotype and phenotype reveal that severe trimethylaminuria is caused by loss of function mutations in FMO3
results show that FMO3 E158K and POR (show POR Antibodies) A503V polymorphisms are minor sources of nicotine metabolism variation, insufficient to appreciably alter smoking.
CYP3A4 (show CYP3A4 Antibodies) and FMO3 are the major enzymes responsible for the metabolism of teneligliptin in humans.
Fishy off-flavor in cow's milk is caused by a nonsense mutation (R238X) in FMO3, found to be surprisingly common (q = 0.155) in the Swedish Red and White breed of dairy cattle.
FMO3 is increased in obese/insulin (show INS Antibodies) resistant male mice and necessary for expression of FoxO1 (show FOXO1 Antibodies).
Fmo3 expression and function plays a role in protecting the liver from acetaminophen-induced toxicity.
a major role for FMO3 in modulating glucose and lipid homeostasis
Report temporal changes in hepatic Fmo3 gene expression under different conditions all known to cause hepatic oxidative stress.
Report selective modulation of hepatic cytochrome P450 (show CYP Antibodies) and flavin monooxygenase 3 expression during citrobacter rodentium infection in SCID (show PRKDC Antibodies) mice.
The functional activity of Fmo3 was determined.
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 the same protein. 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.
dimethylaniline monooxygenase [N-oxide-forming] 3
, flavin containing monooxygenase 3
, FMO 3
, FMO II
, FMO form 2
, dimethylaniline oxidase 3
, hepatic flavin-containing monooxygenase 3
, hepatic flavin-containing monooxygenase-3
, trimethylamine monooxygenase
, flavin-containing monooxygenase 3
, FMO 1D1
, flavin-containing monooxygenase FMO3
, flavin-containing monooxygenase form 3