DLD Lentiviral Activation Particles (h): sc-403207-LAC

Human DLD encodes dihydrolipoamide dehydrogenase, a mitochondrial FAD-dependent oxidoreductase that regenerates oxidized lipoamide to sustain catalytic cycling of multiple dehydrogenase complexes. As the E3 subunit shared by pyruvate dehydrogenase, α‑ketoglutarate dehydrogenase, and branched-chain α‑ketoacid dehydrogenase, DLD links glycolytic carbon entry and TCA cycle flux with amino acid catabolism and redox homeostasis through NADH production. DLD activity contributes to mitochondrial energy metabolism and reactive oxygen species balance, connecting it to pathways that shape metabolic stress responses. Genetic or functional perturbation of DLD has been associated with mitochondrial metabolic disorders and altered cellular bioenergetics, supporting its use in studies of neurometabolic phenotypes and mitochondrial dysfunction mechanisms.

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

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