FMO1 Antibody (Center)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, IHC-P, FC, E |
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Primary Accession | Q01740 |
Reactivity | Human |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 60311 Da |
Antigen Region | 391-417 aa |
Gene ID | 2326 |
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Other Names | Dimethylaniline monooxygenase [N-oxide-forming] 1, Dimethylaniline oxidase 1, Fetal hepatic flavin-containing monooxygenase 1, FMO 1, FMO1 |
Target/Specificity | This FMO1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 391-417 amino acids from the Central region of human FMO1. |
Dilution | WB~~1:1000 IHC-P~~1:50~100 FC~~1:10~50 |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | FMO1 Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | FMO1 (HGNC:3769) |
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Function | Broad spectrum monooxygenase that catalyzes the oxygenation of a wide variety of nitrogen- and sulfur-containing compounds including xenobiotics (PubMed:32156684). Catalyzes the S-oxygenation of hypotaurine to produce taurine, an organic osmolyte involved in cell volume regulation as well as a variety of cytoprotective and developmental processes (PubMed:32156684). In vitro, catalyzes the N- oxygenation of trimethylamine (TMA) to produce trimethylamine N-oxide (TMAO) and could therefore participate to the detoxification of this compound that is generated by the action of gut microbiota from dietary precursors such as choline, choline containing compounds, betaine or L- carnitine (By similarity). |
Cellular Location | Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P36365}; Single-pass membrane protein |
Tissue Location | Expressed mainly in fetal and adult liver. |
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Provided below are standard protocols that you may find useful for product applications.
Background
Metabolic N-oxidation of the diet-derived amino-trimethylamine (TMA) is mediated by flavin-containing monooxygenase and is subject to an inherited FMO3 polymorphism in man resulting in a small subpopulation with reduced TMA N-oxidation capacity resulting in fish odor syndrome Trimethylaminuria. Three forms of the enzyme, FMO1 found in fetal liver, FMO2 found in adult liver, and FMO3 are encoded by genes clustered in the 1q23-q25 region. Flavin-containing monooxygenases are NADPH-dependent flavoenzymes that catalyzes the oxidation of soft nucleophilic heteroatom centers in drugs, pesticides, and xenobiotics.
References
Hines,R.N. et.al., Expert Opin Drug Metab Toxicol 2 (1), 41-49 (2006)
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