NQO1 Lentiviral Activation Particles (h): sc-400326-LAC

NQO1 (NAD(P)H quinone dehydrogenase 1) is a cytosolic flavoprotein that catalyzes the two-electron reduction of quinones to hydroquinones, limiting redox cycling and reactive oxygen species generation. As a canonical NRF2/KEAP1-regulated detoxification enzyme, NQO1 supports cellular redox homeostasis and intersects with xenobiotic metabolism, oxidative stress responses, and proteostasis via stabilization of select proteins. Altered NQO1 expression and activity have been linked to variation in susceptibility to oxidative damage and to context-dependent tumor biology, making it relevant for mechanistic studies in carcinogenesis and stress adaptation. NQO1 is also frequently used as a readout for pathway activation in antioxidant response element (ARE) signaling and electrophile-induced transcriptional programs.

NQO1 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 NQO1 upregulation across a broader range of human cell types.

NQO1 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 NQO1 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous NQO1 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native NQO1 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.