quiescin Q6 CRISPR Activation Plasmid (h): sc-405059-ACT

Human QSOX1 encodes quiescin Q6, a FAD-dependent sulfhydryl oxidase that catalyzes disulfide bond formation and contributes to oxidative protein folding in the secretory pathway and extracellular matrix. By generating disulfide bonds and producing hydrogen peroxide as a byproduct, QSOX1 influences redox homeostasis, protein maturation, and matrix remodeling processes that affect cell adhesion and migration. QSOX1 activity has been linked to changes in tumor microenvironment organization, fibrotic remodeling, and inflammatory signaling contexts, making it a useful node for studying disease-associated extracellular proteostasis. Its expression and function are also relevant to stress-adaptive pathways that coordinate secretion, ER/secretory trafficking, and redox-dependent signaling.

quiescin Q6 CRISPR Activation Plasmid (h) provides a targeted, non-destructive approach to upregulating endogenous QSOX1 expression without altering the underlying DNA sequence.

quiescin Q6 CRISPR Activation Plasmid (h) is a three-plasmid synergistic activation mediator (SAM) system engineered for highly efficient, site-specific transcriptional upregulation of the QSOX1 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 QSOX1 transcriptional start site, where VP64, p65, and HSF1 act in concert to recruit transcriptional machinery and drive upregulation of endogenous quiescin Q6 expression. Unlike nuclease-active Cas9, dCas9 does not introduce double-strand breaks or modify the genomic sequence, preserving the native QSOX1 locus and enabling the study of quiescin Q6-dependent transcriptional responses at the endogenous locus, making it a valuable tool for functional studies, target gene identification, and the modeling of quiescin Q6 pathway restoration in tumor cells with silenced or reduced QSOX1 expression.

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