SULT1A3/1A4 CRISPR Activation Plasmid (h): sc-417824-ACT

Human SULT1A3/1A4 encode closely related cytosolic sulfotransferases that catalyze sulfate conjugation of catecholamines and other phenolic monoamines, shaping the balance between bioactive and inactivated metabolites. By generating sulfated products, SULT1A3/1A4 participate in phase II xenobiotic metabolism and intersect with neurotransmitter turnover and cellular redox homeostasis through modulation of catechol-derived reactive intermediates. Their activity influences tissue- and cell-type–specific handling of dopamine and related substrates, linking metabolic capacity to signaling tone. Altered sulfation capacity has been investigated in the context of neuropsychiatric phenotypes, stress responses, and variable drug metabolism, making SULT1A3/1A4 useful markers for studying metabolic heterogeneity.

SULT1A3/1A4 CRISPR Activation Plasmid (h) provides a targeted, non-destructive approach to upregulating endogenous SULT1A3 expression without altering the underlying DNA sequence.

SULT1A3/1A4 CRISPR Activation Plasmid (h) is a three-plasmid synergistic activation mediator (SAM) system engineered for highly efficient, site-specific transcriptional upregulation of the SULT1A3 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 SULT1A3 transcriptional start site, where VP64, p65, and HSF1 act in concert to recruit transcriptional machinery and drive upregulation of endogenous SULT1A3/1A4 expression. Unlike nuclease-active Cas9, dCas9 does not introduce double-strand breaks or modify the genomic sequence, preserving the native SULT1A3 locus and enabling the study of SULT1A3/1A4-dependent transcriptional responses at the endogenous locus, making it a valuable tool for functional studies, target gene identification, and the modeling of SULT1A3/1A4 pathway restoration in tumor cells with silenced or reduced SULT1A3 expression.

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