PDE1C is a member of the phosphodiesterases (PDE) family which catalyzes the hydrolysis of cyclic nucleotides cAMP and cGMP to the corresponding nucleoside 5-prime-monophosphates. PDE1C binds both cAMP and cGMP with high affinity and hydrolyzes both substrates with similar rates of catalysis (1). PDE1C is a calmodulin-dependent PDE and is stimulated by calcium-calmodulin complex. PDE1C is expressed at high levels in human cardiac myocytes with an intracellular distribution distinct from that of other phosphodiesterases (2). PDE1C levels decrease in all conditions that inhibited cell proliferation and PDE1C is a useful marker in studying the dynamics of proliferation and migration of various cells.
1. Loughney, K. et al: Isolation and characterization of cDNAs corresponding to two human calcium, calmodulin-regulated, 3-prime, 5-prime-cyclic nucleotide phosphodiesterases. J. Biol. Chem. 271: 796-806, 1996.
2. Vandeput, F. et al; Cyclic nucleotide phosphodiesterase PDE1C1 in human cardiac myocytes. J. Biol. Chem. 282: 32749-42757, 2007.
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