PPARα Lentiviral Activation Particles (h): sc-400238-LAC

PPARA encodes peroxisome proliferator-activated receptor alpha (PPARα), a ligand-activated nuclear receptor that regulates transcriptional programs controlling lipid uptake, mitochondrial and peroxisomal β-oxidation, and ketogenesis. PPARα functions as a heterodimer with RXR and binds PPAR response elements to coordinate metabolic adaptation during fasting and high fatty-acid flux, integrating signals from fatty acids and eicosanoids. It interfaces with pathways governing lipoprotein metabolism, bile acid homeostasis, and inflammatory gene expression via crosstalk with NF-κB and other transcriptional regulators. Dysregulated PPARα signaling has been implicated in metabolic dysfunction states including dyslipidemia and fatty liver phenotypes, and is frequently studied in the context of cardiometabolic stress responses.

PPARα 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 PPARA upregulation across a broader range of human cell types.

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