GSTO1 Lentiviral Activation Particles (h): sc-404107-LAC

Glutathione S-transferase omega 1 (GSTO1) is a cytosolic thioltransferase with deglutathionylase and redox-modulating activities that distinguish it from canonical GST enzymes. By regulating glutathione-dependent detoxification reactions and protein S-glutathionylation status, GSTO1 influences cellular antioxidant defenses, inflammatory signaling, and proteostasis under oxidative stress. Its activity has been linked to modulation of pathways involving reactive oxygen species handling, xenobiotic metabolism, and redox-sensitive transcriptional programs. Altered GSTO1 expression or function is studied in the context of neurodegeneration, cardiometabolic stress responses, and cancer-associated redox adaptation, where shifts in redox homeostasis can shape disease-relevant phenotypes.

GSTO1 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 GSTO1 upregulation across a broader range of human cell types.

GSTO1 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 GSTO1 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous GSTO1 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native GSTO1 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.