Full length protein corresponding to Human FMO2 aa 1-471. (NP_001451.1).Sequence: MAKKVAVIGAGVSGLISLKCCVDEGLEPTCFERTEDIGGVWRFKENVEDG RASIYQSVVTNTSKEMSCFSDFPMPEDFPNFLHNSKLLEYFRIFAKKFDL LKYIQFQTTVLSVRKCPDFSSSGQWKVVTQSNGKEQSAVFDAVMVCSGHH ILPHIPLKSFPGMERFKGQY
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.
Pathway
Biological oxidations; Drug metabolism - cytochrome P450; FMO oxidizes nucleophiles; Metabolism; Phase 1 - Functionalization of compounds; nicotine degradation II;
Custom Antibody Labeling
We offer labeled antibodies using our catalogue antibody products and a broad range of intensely fluorescent dyes and labels including HRP, biotin, ALP, Alexa Fluor® dyes, DyLight® Fluor dyes, R-phycoerythrin (R-PE), at scales from less than 100 μg up to 1 g of IgG antibody. Learn More
Citations
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Wyatt, MK; Overby, LH; et al. Identification of amino acid residues associated with modulation of flavin-containing monooxygenase (FMO) activity by imipramine: Structure/function studies with FMO1 from pig and rabbit. BIOCHEMISTRY 37:5930-5938(1998).
Yueh, MF; Krueger, SK; et al. Pulmonary flavin-containing monooxygenase (FMO) in Rhesus macaque: Expression of FMO2 protein, mRNA and analysis of the cDNA. BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION 1350:267-271(1997).
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COA
Certificate of Analysis