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FMO2 Antibody (C-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | Q99518 |
|---|---|
| Clone Names | 81020096 |
| Gene ID | 2327 |
|---|---|
| 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 | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| 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. |
| Name | FMO2 (HGNC:3770) |
|---|---|
| Function | Catalyzes the oxidative metabolism of numerous xenobiotics, including mainly therapeutic drugs and insecticides that contain a soft nucleophile, most commonly nitrogen and sulfur and participates to their bioactivation (PubMed:9804831, PubMed:15294458, PubMed:15144220, PubMed:18948378, PubMed:18930751). Specifically catalyzes S-oxygenation of sulfur derived compounds such as thioureas-derived compounds, thioetherorganophosphates to their sulfenic acid (PubMed:9804831, PubMed:15144220). In vitro, catalyzes S-oxygenation of the second-line antitubercular drugs thiacetazone (TAZ) and ethionamide (ETA), forming a sulfinic acid and a carbodiimide via a postulated sulfenic acid intermediate (PubMed:18948378, PubMed:18930751). Also catalyzes S- oxygenation of the thioether-containing organophosphate insecticides, phorate and disulfoton (PubMed:15294458). |
| Cellular Location | Microsome membrane {ECO:0000250|UniProtKB:P17635}; Single-pass membrane protein. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17635}; Single-pass membrane protein |
| 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.
Background
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.
References
Krueger,S.K., Pharmacogenet. Genomics 15 (4), 245-256 (2005)
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