PDE1B1 (human, recombinant)

Phosphodiesterase 1B (PDE1B) is a calcium/calmodulin-stimulated cyclic nucleotide phosphodiesterase that hydrolyzes both cAMP and cGMP. Alternative splicing of PDE1B pre-mRNA results in the formation of various PDE1B isoforms, including PDE1B1. PDE1B1 is comprised of an N-terminal calmodulin binding domain, a catalytic domain, and a C-terminal domain. PDE1B1 is expressed in the brain, with the highest levels observed in the caudate nucleus and putamen. PDE1B knockout mice have decreased striatal serotonin levels and exhibit increased spontaneous locomotor activity in a novel environment, as well as increased methamphetamine-induced locomotor activity compared with wild-type mice. Striatal expression of PDE1B is decreased in the R6/2 transgenic mouse model of Huntington's disease. Cayman's PDE1B1 (human, recombinant) protein consists of 773 amino acids and has a calculated molecular weight of 89.2 kDa.Synonyms: Calcium/Calmodulin-dependent 3',5'-Cyclic Nucleotide Phosphodiesterase 1B, Cam-PDE 1B, Phosphodiesterase 1B1. Purity: >94% estimated by SDS-PAGE. Endotoxin Testing: <1.0 EU/µg, determined by the LAL endotoxin assay. Source: Recombinant human N-terminal His-GST-tagged PDE1B1 expressed in insect cells. Amino Acids: 1-536 (full length). MW: 89.2 kDa. Formulation: (Request formulation change), Lyophilized from sterile 50 mM Tris, pH 8.0, with 100 mM sodium chloride. UniProt Accession #: Q01064-1.