G6PD Lentiviral Activation Particles (h): sc-401019-LAC

Glucose-6-phosphate dehydrogenase (G6PD) is the rate-limiting enzyme of the oxidative branch of the pentose phosphate pathway, generating NADPH required for glutathione reduction, reactive oxygen species detoxification, and redox homeostasis. In human cells, G6PD activity supports biosynthetic metabolism by supplying ribose-5-phosphate for nucleotide synthesis and reducing equivalents for lipid and nitric oxide metabolism. Perturbations in G6PD expression or enzymatic activity influence susceptibility to oxidative stress, mitochondrial function, and metabolic reprogramming. G6PD deficiency is a common inherited enzymopathy with hematologic sensitivity to oxidative challenges, and altered G6PD regulation is studied in contexts of inflammation, infection biology, and cancer metabolism.

G6PD 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 G6PD upregulation across a broader range of human cell types.

G6PD 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 G6PD transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous G6PD expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native G6PD 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.