Fatty Acid Synthase Lentiviral Activation Particles (h): sc-400440-LAC

Human FASN encodes fatty acid synthase, a multifunctional cytosolic enzyme complex that catalyzes de novo lipogenesis by converting acetyl-CoA and malonyl-CoA into long-chain saturated fatty acids such as palmitate. This activity integrates with central carbon metabolism, NADPH-dependent reductive biosynthesis, and lipid remodeling to support membrane biogenesis, protein acylation, and lipid-derived signaling. FASN function intersects with nutrient-sensing and growth pathways including PI3K–AKT–mTOR signaling and is modulated by transcriptional programs driven by SREBP and related lipogenic regulators. Dysregulated FASN expression and lipogenic flux are frequently associated with metabolic disease states and cancer-associated metabolic reprogramming, making it a key node for studying lipid metabolism and cell-state transitions.

Fatty Acid Synthase 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 FASN upregulation across a broader range of human cell types.

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