Anti-FDPS/FPS Picoband® Antibody Fluoro647 Conjugated

Dimethylallyltranstransferase (DMATT), also known as farnesylpyrophosphate synthase (FPPS) or as farnesyldiphosphate synthase (FDPS), is an enzyme that in humans is encoded by the FDPS gene. It is mapped to 1q22. This gene encodes an enzyme that catalyzes the production of geranyl pyrophosphate and farnesyl pyrophosphate from isopentenyl pyrophosphate and dimethylallyl pyrophosphate. The resulting product, farnesyl pyrophosphate, is a key intermediate in cholesterol and sterol biosynthesis, a substrate for protein farnesylation and geranylgeranylation, and a ligand or agonist for certain hormone receptors and growth receptors. Drugs that inhibit this enzyme prevent the post-translational modifications of small GTPases and have been used to treat diseases related to bone resorption. Multiple pseudogenes have been found on chromosomes 1, 7, 14, 15, 21 and X. Multiple transcript variants encoding different isoforms have been found for this gene.

Farnesyl pyrophosphate synthase; FPP synthase; FPS; (2E,6E) -farnesyl diphosphate synthase; Dimethylallyltranstransferase; Farnesyl diphosphate synthase; Geranyltranstransferase; FDPS; FPS; KIAA1293

Key enzyme in isoprenoid biosynthesis which catalyzes the formation of farnesyl diphosphate (FPP), a precursor for several classes of essential metabolites including sterols, dolichols, carotenoids, and ubiquinones. FPP also serves as substrate for protein farnesylation and geranylgeranylation. Catalyzes the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates, dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate.

1. Heinzmann, C., Clarke, C. F., Klisak, I., Mohandas, T., Sparkes, R. S., Edwards, P. A., Lusis, A. J. Dispersed family of human genes with sequence similarity to farnesyl pyrophosphate synthetase. Genomics 5: 493-500, 1989. 2. Krisans, S. K., Ericsson, J., Edwards, P. A., Keller, G. A. Farnesyl-diphosphate synthase is localized in peroxisomes. J. Biol. Chem. 269: 14165-14169, 1994. 3. Scott, A. F. Personal Communication. Baltimore, Md. 11/9/2006.