PDE1C antibody

Background of PDE1C antibody

Cyclic nucleotides are hydrolyzed and compartmentalized by a family of enzymes called phosphodieterases. In mammals at least 11 different families of PDEs can be discriminated (PDE1-PDE11) based on their kinetic properties and inhibition to various pharmacological agents. Three different PDE1 genes have been identified (PDE1A, PDE1B, PDE1C). The enzymes of the PDE1A and PDE1B have higher affinity for cGMP than for cAMP, where as, Pde1C has high affinity for both cAMP and cGMP. Calcium-Calmodulin stimulates the activity of each of these enzymes several-fold. The PDE1C gene has been cloned from human, mouse and rat. The PDE1C gene codes a family of proteins (variants) that differ from each other at amino and carboxy termini of the protein. The predicted size of PDE1C gene products ranged between 70-87 kDa. Members of the PDE1C gene have a longer carboxy terminus that accounts for their larger size. The tissue distribution of PDE1C is different from other PDE1 gene family members. A 5’ splice variant of PDE1C2 is found in rat olfactory epithelium (Yan and Beavo 1994; Yan et. al., 1995) and is believed to be involved in olfactory signal transduction. Other PDE1C variants (PDE1C1 and PDE1C2) are found in human heart (Loughney et. al., 1996). The PDE1C enzymes bind both cGMP and cAMP with different affinities. The phosphodiesterase type-1C has at least three variants (PDE1C1, PDE1C2, PDE1C3) ranging in molecular weight between 70-87 kDa. PDE1C is 634 amino acids long and has at least three splice variants that are expressed in heart, olfactory epithelium and other brain regions, lungs and testis.