PDE1B1 (human, recombinant)

Phosphodiesterase 1B (PDE1B) is a calcium/calmodulin-stimulated cyclic nucleotide phosphodiesterase that hydrolyzes both cAMP and cGMP.¹ Alternative splicing of PDE1B pre-mRNA results in the formation of various PDE1B isoforms, including PDE1B1.² PDE1B1 is comprised of an N-terminal calmodulin binding domain, a catalytic domain, and a C-terminal domain.¹ PDE1B1 is expressed in the brain, with the highest levels observed in the caudate nucleus and putamen.² 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.³ Striatal expression of PDE1B is decreased in the R6/2 transgenic mouse model of Huntington's disease.⁴ Cayman's PDE1B1 (human, recombinant) protein consists of 773 amino acids and has a calculated molecular weight of 89.2 kDa.

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1. Yu, J., Wolda, S.L., Frazier, A.L.B., et al. Identification and characterisation of a human calmodulin-stimulated phosphodiesterase PDE1B1. Cell Signal. 9(7), 519-529 (1997).

2. Fidock, M., Miller, M., and Lanfear, J. Isolation and differential tissue distribution of two human cDNAs encoding PDE1 splice variants. Cell Signal. 14(1), 53-60 (2002).

3. Siuciak, J.A., McCarthy, S.A., Chapin, D.S., et al. Behavioral and neurochemical characterization of mice deficient in the phosphodiesterase-1B (PDE1B) enzyme. Neuropharmacology 53(1), 113-124 (2007).

4. Hebb, A.L.O., Robertson, H.A., and Denovan-Wright, E.M. Striatal phosphodiesterase mRNA and protein levels are reduced in Huntington’s disease transgenic mice prior to the onset of motor symptoms. Neuroscience 123(4), 967-981 (2004).