Anti-CYP26A1 Antibody Picoband® Fluoro647 Conjugated

Cytochrome P450 26A1 is a protein that in humans is encoded by the CYP26A1 gene. This gene encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This endoplasmic reticulum protein acts on retinoids, including all-trans-retinoic acid (RA), with both 4-hydroxylation and 18-hydroxylation activities. This enzyme regulates the cellular level of retinoic acid which is involved in regulation of gene expression in both embryonic and adult tissues. Two alternatively spliced transcript variants of this gene, which encode the distinct isoforms, have been reported.

Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Interacts with MCMBP.

1. Kinkel, M. D., Sefton, E. M., Kikuchi, Y., Mizoguchi, T., Ward, A. B., Prince, V. E. Cyp26 enzymes function in endoderm to regulate pancreatic field size. Proc. Nat. Acad. Sci. 106: 7864-7869, 2009. 2. Lee, S.-J., Perera, L., Coulter, S. J., Mohrenweiser, H. W., Jetten, A., Goldstein, J. A. The discovery of new coding alleles of human CYP26A1 that are potentially defective in the metabolism of all-trans retinoic acid and their assessment in a recombinant cDNA expression system. Pharmacogenet. Genomics 17: 169-180, 2007. 3. Niederreither, K., Abu-Abed, S., Schuhbaur, B., Petkovich, M., Chambon, P., Dolle, P. Genetic evidence that oxidative derivatives of retinoic acid are not involved in retinoid signaling during mouse development. Nature Genet. 31: 84-88, 2002.