Superoxide Dismutase 1/SOD1 Lentiviral Activation Particles (h): sc-400186-LAC

Human SOD1 encodes cytosolic Cu/Zn superoxide dismutase, a key antioxidant enzyme that catalyzes the conversion of superoxide radicals into hydrogen peroxide and molecular oxygen to preserve redox homeostasis. By limiting reactive oxygen species accumulation, SOD1 influences mitochondrial function, proteostasis, and stress-response signaling pathways such as NRF2-regulated antioxidant programs and redox-sensitive inflammatory signaling. Altered SOD1 activity or misfolding is linked to oxidative damage and neuronal vulnerability, with well-established relevance to amyotrophic lateral sclerosis (ALS) and broader neurodegeneration models. SOD1 is also widely studied in cancer, ischemia-reperfusion injury, and metabolic stress contexts where reactive oxygen species shape cell survival, differentiation, and signaling.

Superoxide Dismutase 1/SOD1 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 SOD1 upregulation across a broader range of human cell types.

Superoxide Dismutase 1/SOD1 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 SOD1 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous Superoxide Dismutase 1/SOD1 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native SOD1 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.