FMO5 (Dimethylaniline oxidase 5:Hepatic flavin-containing monooxygenase 5)

Dimethylaniline monooxygenase [N-oxide-forming] 5 also known as FMO 5 is an enzyme that in humans is encoded by the FMO5 gene. By fluorescence in situ hybridization, this gene was assigned to human chromosome 1q21.1. FMO5 is not an efficient drug-metabolizing enzyme and that it may have an alternative physiologic role. FMO5 transcripts play an important role in progesterone-regulated in breast cancer cells specifically under the control of the progesterone receptor B-isoform.\n\nUniProt Number:\nP49326\n\nGene ID:\nFMO5\n\nApplications:\nSuitable for use in Western Blot.\n\nRecommended Dilution:\nOptimal dilutions to be determined by the researcher.\n\nStorage and Handling:\nStore at -20?C for one year. After reconstitution, store at 4?C for one month. Can also be aliquoted and stored frozen at -20?C for long term.\nAvoid repeated freezing and thawing. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

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SPECIFICATIONS

Catalog Number

144546

Size

100ug

Applications

WB

Hosts

Rabbit

Reactivities

Hum, Mouse, Rat

Form

Supplied as a lyophilized powder. Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg Thimerosal, 0.05mg NaN3. Reconstitution: Add 0.2ml of distilled water will yield a concentration of 500ug/ml.

P Type

Pab

Purity

Purified by immunoaffinity chromatography.

Isotype

IgG

References

1. Gelb, B. D., Zhang, J., Cotter, P. D., Gershin, I. F., Desnick, R. J. Physical mapping of the human connexin 40 (GJA5), flavin-containing monooxygenase 5, and natriuretic peptide receptor A genes on 1q21. Genomics 39: 409-411, 1997.\n2. Miller, M. M., James, R. A., Richer, J. K., Gordon, D. F., Wood, W. M., Horwitz, K. B.Progesterone regulated expression of flavin-containing monooxygenase 5 by the B-isoform of progesterone receptors: implications for tamoxifen carcinogenicity. J. Clin. Endocr. Metab. 82: 2956-2961, 1997.\n3. Overby, L. H., Buckpitt, A. R., Lawton, M. P., Atta-Asafo-Adjei, E., Schulze, J., Philpot, R. M. Characterization of flavin-containing monooxygenase 5(FMO5) cloned from human and guinea pig: evidence that the unique catalytic properties of FMO5 are not confined to the rabbit ortholog. Arch. Biochem. Biophys. 317: 275-284, 1995. \n

Additional Info

Recognizes human,mouse and rat FMO5. No crossreactivity with other proteins.