PDE10A is a member of the phosphodiesterase family of proteins that play a critical role in regulating intracellular levels of cAMP and cGMP (1). PDE10A eliminates cAMP- and cGMP-mediated intracellular signaling by hydrolyzing the cyclic nucleotide to the corresponding nucleoside 5-prime monophosphate. PDE10A hydrolyzes cAMP and cGMP in transfected COS-7 cells (2). PDE10A has a 11-fold higher affinity for cGMP than cAMP and cAMP can efficiently inhibit cGMP phosphodiesterase activity of PDE10A. PDE10A is being used as a biomarker in clinical trials of gene-disease association and gene-environment interaction.
HSPDE10A; FLJ11894; FLJ25677
1. Fujishige, K. et.al: Cloning and characterization of a novel human phosphodiesterase that hydrolyzes both cAMP and cGMP (PDE10A). J. Biol. Chem. 274: 18438-18445, 1999.
2. Loughney, K et.al: Isolation and characterization of PDE10A, a novel human 3-prime, 5-prime-cyclic nucleotide phosphodiesterase. Gene 234: 109-117, 1999.
Sample Phosphodiesterase Activity Plot. For specific information on a given lot, see related technical data sheet.
Sample Purity Data. For specific information on a given lot, see related technical data sheet.
Storage, Stability and Shipping:
Store product at –70oC. For optimal storage, aliquot target into smaller quantities after centrifugation and store at recommended temperature. For most favorable performance, avoid repeated handling and multiple freeze/thaw cycles.
Cardiovascular Disease, Inflammation, Phosphodiesterases