TERE1 CRISPR Activation Plasmid (h): sc-402125-ACT

UBIAD1 encodes the human TERE1 protein, a prenyltransferase that links the mevalonate pathway to intracellular redox homeostasis through biosynthesis of vitamin K2 (menaquinone-4) and related isoprenoid quinones. By regulating quinone-dependent electron transport and oxidative stress responses, UBIAD1 influences mitochondrial function, lipid metabolism, and membrane-associated signaling processes. Altered UBIAD1 activity has been associated with dysregulated cholesterol handling and corneal lipid deposition in Schnyder corneal dystrophy, and its broader roles in cellular proliferation and stress adaptation make it relevant for mechanistic studies of metabolic disease and cancer biology.

TERE1 CRISPR Activation Plasmid (h) provides a targeted, non-destructive approach to upregulating endogenous UBIAD1 expression without altering the underlying DNA sequence.

TERE1 CRISPR Activation Plasmid (h) is a three-plasmid synergistic activation mediator (SAM) system engineered for highly efficient, site-specific transcriptional upregulation of the UBIAD1 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 UBIAD1 transcriptional start site, where VP64, p65, and HSF1 act in concert to recruit transcriptional machinery and drive upregulation of endogenous TERE1 expression. Unlike nuclease-active Cas9, dCas9 does not introduce double-strand breaks or modify the genomic sequence, preserving the native UBIAD1 locus and enabling the study of TERE1-dependent transcriptional responses at the endogenous locus, making it a valuable tool for functional studies, target gene identification, and the modeling of TERE1 pathway restoration in tumor cells with silenced or reduced UBIAD1 expression.

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