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Anti-FMO2 Picoband Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB |
|---|---|
| Primary Accession | Q99518 |
| Host | Rabbit |
| Reactivity | Human |
| Clonality | Polyclonal |
| Format | Lyophilized |
| Description | Rabbit IgG polyclonal antibody for Dimethylaniline monooxygenase [N-oxide-forming] 2(FMO2) detection. Tested with WB in Human. |
| Reconstitution | Add 0.2ml of distilled water will yield a concentration of 500ug/ml. |
| Gene ID | 2327 |
|---|---|
| Other Names | Dimethylaniline monooxygenase [N-oxide-forming] 2, 1.14.13.8, Dimethylaniline oxidase 2, FMO 1B1, Pulmonary flavin-containing monooxygenase 2, FMO 2, FMO2 |
| Calculated MW | 53644 MW KDa |
| Application Details | Western blot, 0.1-0.5 µg/ml, Human |
| Subcellular Localization | Microsome membrane. Endoplasmic reticulum membrane. |
| Tissue Specificity | 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. . |
| Protein Name | Dimethylaniline monooxygenase [N-oxide-forming] 2 |
| Contents | Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg NaN3. |
| Immunogen | A synthetic peptide corresponding to a sequence at the N-terminus of human FMO2 (78-115aa FPNFLHNSKLLEYFRIFAKKFDLLKYIQFQTTVLSVRK), different from the related mouse and rat sequences by two amino acids. |
| Purification | Immunogen affinity purified. |
| Cross Reactivity | No cross reactivity with other proteins. |
| Storage | At -20˚C for one year. After r˚Constitution, at 4˚C for one month. It˚Can also be aliquotted and stored frozen at -20˚C for a longer time.Avoid repeated freezing and thawing. |
| 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
Dimethylaniline monooxygenase [N-oxide-forming] 2 is an enzyme that in humans is encoded by the FMO2 gene. This gene encodes a flavin-containing monooxygenase family member. It is an NADPH-dependent enzyme that catalyzes the N-oxidation of some primary alkylamines through an N-hydroxylamine intermediate. However, some human populations contain an allele (FMO2*2A) with a premature stop codon, resulting in a protein that is C-terminally-truncated, has no catalytic activity, and is likely degraded rapidly. This gene is found in a cluster with other related family members on chromosome 1. Alternative splicing results in multiple transcript variants.
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