PRODH Lentiviral Activation Particles (h): sc-403063-LAC

Human PRODH encodes proline dehydrogenase (proline oxidase), a mitochondrial inner membrane flavoprotein that catalyzes the first step of proline catabolism, converting proline to Δ1-pyrroline-5-carboxylate and transferring electrons to the respiratory chain. Through the proline–P5C redox shuttle, PRODH links amino acid metabolism with cellular redox balance, mitochondrial function, and bioenergetic homeostasis. Altered PRODH activity has been associated with perturbations in oxidative stress signaling and metabolic rewiring, with relevance to neuropsychiatric phenotypes and cancer-related metabolic programs. As a pathway node bridging proline metabolism, ROS production, and mitochondrial respiration, PRODH is frequently examined in studies of stress adaptation and metabolic regulation.

PRODH 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 PRODH upregulation across a broader range of human cell types.

PRODH 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 PRODH transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous PRODH expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native PRODH 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.