|Other Names||Dimethylaniline monooxygenase [N-oxide-forming] 2, Dimethylaniline oxidase 2, FMO 1B1, Pulmonary flavin-containing monooxygenase 2, FMO 2, FMO2|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP6645b was selected from the C-term region of human FMO2. 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||Catalyzes the N-oxidation of certain primary alkylamines to their oximes via an N-hydroxylamine intermediate. Inactive toward certain tertiary amines, such as imipramine or chloropromazine. Can catalyze the S-oxidation of methimazole. The truncated form is catalytically inactive.|
|Cellular Location||Microsome membrane. Endoplasmic reticulum membrane|
|Tissue Location||Expressed in lung (at protein level). Expressed predominantly in lung, and at a much lesser extent in kidney. Also expressed in fetal lung, but not in liver, kidney and brain.|
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Provided below are standard protocols that you may find useful for product applications.
The flavin-containing monooxygenases are NADPH-dependent enzymes that catalyze the oxidation of many drugs and xenobiotics. In most mammals, there is a flavin-containing monooxygenase that catalyzes the N-oxidation of some primary alkylamines through an N-hydroxylamine intermediate. However, in humans, this enzyme is truncated and is probably rapidly degraded. The protein represents the truncated form and apparently has no catalytic activity.
Krueger,S.K., Pharmacogenet. Genomics 15 (4), 245-256 (2005)
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