Cayman PDE2A (human, recombinant; aa 215-900)

Phosphodiesterase 2A (PDE2A) is a cGMP-stimulated cyclic nucleotide phosphodiesterase that hydrolyzes cGMP and cAMP. It is a 941-amino acid protein comprised of an N-terminal domain (1-214), GAF-A domain (215-372), GAF-B domain (393-541), and a catalytic domain (579-941) and functions as a homodimer. PDE2A is expressed in the brain and to a lesser extent in heart, placenta, lung, skeletal muscle, kidney, spleen, and pituitary. Upon cGMP binding to the GAF-B domain, PDE2A is activated and hydrolyzes cAMP and cGMP to regulate cell signaling. PDE2A mRNA levels are reduced in postmortem amygdala from patients with schizophrenia, bipolar disorder, and major depressive disorder compared with healthy controls. PDE2A brain activity is increased in the Fmr1^-/- mouse model of fragile X syndrome and administration of the selective PDE2A inhibitor BAY 60-7550 (Item No. ) restores axonal length and spine maturation and attenuates social discriminatory and vocalization deficits in Fmr1^-/- young mice. Adenovirus shRNA knockdown of Pde2a attenuates bronchoalveolar lavage fluid (BALF) neutrophilia, reduces lung levels of inducible nitric oxide synthase (iNOS), and increases lung cAMP levels in a mouse model of acute lung injury. Cayman’s PDE2A (human, recombinant; aa 215-900) protein consists of 706 amino acids and has a calculated molecular weight of 80 kDa. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is 66 kDa.

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