| Form | Liquid |
|---|---|
| Host Species | Rabbit |
| Clonality | Polyclonal |
| Isotype | IgG |
| Purification | Purified by antigen affinity column. |
| Endotoxin Level | Please contact with the lab for this information. |
| Applications | ELISA, IHC, WB |
| Species Reactivity | Human |
| Target | Baeyer-Villiger monooxygenase 1, Dimethylaniline monooxygenase [N-oxide-forming] 5, Dimethylaniline oxidase 5, EC:1.14.13.-, EC:1.14.13.8, EC:1.6.3.1, FMO 5, FMO5, Flavin-containing monooxygenase 5, N |
| Immunogen | E. coli - derived recombinant Human FMO5 (Met1-Ser512). |
| Storage Buffer | 0.01M PBS, pH 7.4, 50% Glycerol, 0.05% Proclin 300. |
| Product Usage Information | ELISA:1:5000-1:20000;IHC:1:50-1:500;WB:1:500-1:2000 |
| Accession Number | P49326 |
| Background | Flavin-containing monooxygenase 5 (FMO5) is a ~60 kDa protein. Acts as a Baeyer-Villiger monooxygenase on a broad range of substrates. Catalyzes the insertion of an oxygen atom into a carbon-carbon bond adjacent to a carbonyl, which converts ketones to esters. Active on diverse carbonyl compounds, whereas soft nucleophiles are mostly non- or poorly reactive. In contrast with other forms of FMO it is non- or poorly active on 'classical' substrates such as drugs, pesticides, and dietary components containing soft nucleophilic heteroatoms (Probable). Able to oxidize drug molecules bearing a carbonyl group on an aliphatic chain, such as nabumetone and pentoxifylline. 1. Lai, WG. et al. (2011) Drug metabolism and disposition: the biological fate of chemicals 39, 61-70. PMID: 20947616 2. Fiorentini, F. et al. (2016) ACS chemical biology 11, 1039-48. PMID: 26771671 3. Fiorentini, F. et al. (2017) ACS chemical biology 12, 2379-2387. PMID: 28783300 4. Overby, LH. et al. (1995) Archives of biochemistry and biophysics 317, 275-84. PMID: 7872795 |
| Note | For research use only |