Grx1 Lentiviral Activation Particles (h): sc-418056-LAC

Human GLRX encodes glutaredoxin-1 (Grx1), a cytosolic thiol–disulfide oxidoreductase that uses glutathione to reverse protein S-glutathionylation and maintain redox homeostasis. Grx1 modulates the cellular response to oxidative and nitrosative stress, shaping signaling outputs in pathways such as NF-κB and MAPK, and influencing apoptosis, inflammation, and metabolic adaptation. By regulating reversible cysteine modifications on target proteins, GLRX helps control mitochondrial function, cytoskeletal dynamics, and antioxidant capacity. Dysregulated GLRX/Grx1 activity and altered S-glutathionylation patterns are associated with disease-relevant processes including chronic inflammation, cardiovascular and neurodegenerative stress responses, and tumor biology.

Grx1 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 GLRX upregulation across a broader range of human cell types.

Grx1 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 GLRX transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous Grx1 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native GLRX 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.