Anti-PRMT6 Antibody Picoband® Fluoro488 Conjugated

Protein arginine N-methyltransferase 6 is an enzyme that in humans is encoded by the PRMT6 gene. The protein encoded by this gene belongs to the arginine N-methyltransferase family, which catalyze the sequential transfer of methyl group from S-adenosyl-L-methionine to the side chain nitrogens of arginine residues within proteins, to form methylated arginine derivatives and S-adenosyl-L-homocysteine. This protein can catalyze both, the formation of omega-N monomethylarginine and asymmetrical dimethylarginine, with a strong preference for the latter. It specifically mediates the asymmetric dimethylation of Arg2 of histone H3, and the methylated form represents a specific tag for epigenetic transcriptional repression. This protein also forms a complex with, and methylates DNA polymerase beta, resulting in stimulation of polymerase activity by enhancing DNA binding and processivity.

Peroxisomal multifunctional enzyme type 2; MFE-2;17-beta-hydroxysteroid dehydrogenase 4;17-beta-HSD 4; D-bifunctional protein; DBP; Multifunctional protein 2; MPF-2; Short chain dehydrogenase/reductase family 8C member 1; (3R) -hydroxyacyl-CoA dehydrogenase;1.1.1.n12; Enoyl-CoA hydratase 2;4.2.1.107;4.2.1.119;3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholest-24-enoyl-CoA hydratase; HSD17B4; EDH17B4, SDR8C1

Cancer, Cardiovascular, Fatty Acid Oxidation, Fatty Acids, Lipid and Lipoprotein Metabolism, Lipid Metabolism, Lipids/Lipoproteins, Metabolic Signaling Pathways, Metabolism, Pathways and Processes, Redox Metabolism, Signal Transduction, Tumor Biomarkers

Bifunctional enzyme acting on the peroxisomal beta- oxidation pathway for fatty acids. Catalyzes the formation of 3- ketoacyl-CoA intermediates from both straight-chain and 2-methyl- branched-chain fatty acids. .

1. El-Andaloussi, N., Valovka, T., Toueille, M., Steinacher, R., Focke, F., Gehrig, P., Covic, M., Hassa, P. O., Schar, P., Hubscher, U., Hottiger, M. O. Arginine methylation regulates DNA polymerase beta. Molec. Cell 22: 51-62, 2006. 2. Frankel, A., Yadav, N., Lee, J., Branscombe, T. L., Clarke, S., Bedford, M. T. The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity. J. Biol. Chem. 277: 3537-3543, 2002. 3. Guccione, E., Bassi, C., Casadio, F., Martinato, F., Cesaroni, M., Schuchlautz, H., Luscher, B., Amati, B. Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex are mutually exclusive. Nature 449: 933-937, 2007.