Superoxide Dismutase 3/SOD3 CRISPR Activation Plasmid (h): sc-402505-ACT

Human SOD3 encodes extracellular superoxide dismutase 3, a secreted Cu/Zn metalloenzyme that catalyzes dismutation of superoxide anion to hydrogen peroxide and oxygen in the extracellular space and perivascular matrix. By limiting reactive oxygen species and preserving nitric oxide bioavailability, SOD3 influences redox homeostasis, endothelial signaling, and extracellular matrix remodeling pathways. Altered SOD3 expression or activity has been associated with oxidative stress–driven mechanisms implicated in cardiovascular and pulmonary pathophysiology, inflammatory tissue injury, and tumor microenvironment dynamics. As a key extracellular antioxidant, SOD3 is commonly studied in contexts such as vascular biology, fibrosis, immune cell trafficking, and redox-regulated transcriptional programs.

Superoxide Dismutase 3/SOD3 CRISPR Activation Plasmid (h) provides a targeted, non-destructive approach to upregulating endogenous SOD3 expression without altering the underlying DNA sequence.

Superoxide Dismutase 3/SOD3 CRISPR Activation Plasmid (h) is a three-plasmid synergistic activation mediator (SAM) system engineered for highly efficient, site-specific transcriptional upregulation of the SOD3 locus in human cell lines. The system is built around a catalytically inactive Cas9 (dCas9) carrying two inactivating mutations (D10A and N863A) that eliminate nuclease activity while preserving DNA binding. This dCas9 is fused to VP64, a potent transcriptional activator, and is co-expressed with a blasticidin resistance gene for selection. The second plasmid encodes the MS2-p65-HSF1 fusion protein, a secondary activator complex that works in concert with dCas9-VP64, alongside a hygromycin resistance gene. The third plasmid encodes a target-specific 20 nt sgRNA fused to two MS2 RNA aptamers that recruit the MS2-p65-HSF1 complex to the activation site, accompanied by a puromycin resistance gene. The three plasmids are delivered at a 1:1:1 mass ratio for balanced expression of all system components.

Once assembled at the target locus, the SAM complex binds within approximately 200 bp upstream of the SOD3 transcriptional start site, where VP64, p65, and HSF1 act in concert to recruit transcriptional machinery and drive upregulation of endogenous Superoxide Dismutase 3/SOD3 expression. Unlike nuclease-active Cas9, dCas9 does not introduce double-strand breaks or modify the genomic sequence, preserving the native SOD3 locus and enabling the study of Superoxide Dismutase 3/SOD3-dependent transcriptional responses at the endogenous locus, making it a valuable tool for functional studies, target gene identification, and the modeling of Superoxide Dismutase 3/SOD3 pathway restoration in tumor cells with silenced or reduced SOD3 expression.

For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.