PDE2A Lentiviral Activation Particles (h): sc-401957-LAC

Human PDE2A encodes phosphodiesterase 2A, a dual-substrate cyclic nucleotide phosphodiesterase that hydrolyzes both cAMP and cGMP, thereby shaping second-messenger amplitude and compartmentalization. PDE2A is stimulated by cGMP binding to its regulatory GAF domain, enabling cGMP-to-cAMP cross-talk that influences PKA/PKG signaling, ion channel activity, and phosphorylation-dependent transcriptional responses. Through control of cyclic nucleotide signaling, PDE2A contributes to neuronal excitability and synaptic plasticity as well as cardiovascular and inflammatory signaling programs. Altered PDE2A expression or activity has been associated with neuropsychiatric and neurodegenerative disease biology and with dysregulated cardiometabolic signaling, supporting its utility as a pathway node for mechanistic research.

PDE2A Lentiviral Activation Particles (h) address this need by packaging the complete synergistic activation mediator (SAM) transcriptional activation system into transduction-ready, high-titer lentiviral particles, enabling efficient PDE2A upregulation across a broader range of human cell types.

PDE2A Lentiviral Activation Particles (h) deliver all functional components of the synergistic activation mediator (SAM) system via lentiviral transduction. The system comprises three particle preparations co-transduced into target cells: one encoding catalytically inactive dCas9 (D10A and N863A mutations) fused to the VP64 transactivation domain with a blasticidin resistance gene; one encoding the MS2-p65-HSF1 fusion protein with a hygromycin resistance gene; and one encoding a target-specific 20 nt sgRNA fused to two MS2 RNA aptamers with a puromycin resistance gene. Following lentiviral transduction and genomic integration of the expression cassettes, the SAM components are stably expressed and assemble at the target locus within the proximal promoter region upstream of the PDE2A transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous PDE2A expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native PDE2A genomic locus and regulatory architecture.

The lentiviral format offers several practical advantages: stable genomic integration supports heritable activation across cell divisions; high-titer particle preparations eliminate the need for in-house viral production; and compatibility with primary, non-dividing, and transfection-resistant cell types expands experimental accessibility. Successful transduction can be confirmed and enriched through triple antibiotic selection using puromycin, hygromycin, and blasticidin.

For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.