SULT2B1 CRISPR Activation Plasmid (m): sc-424817-ACT

Mouse Sult2b1 encodes the cytosolic sulfotransferase SULT2B1, an enzyme that catalyzes 3′-phosphoadenosine-5′-phosphosulfate (PAPS)-dependent sulfation of sterols such as cholesterol and oxysterols. By regulating the balance of active versus sulfated sterol pools, SULT2B1 influences steroid/sterol metabolism, lipid homeostasis, and signaling nodes coupled to nuclear receptor pathways including LXR and related transcriptional programs. Sult2b1 activity has been linked to barrier lipid biology in epithelial tissues and to immunometabolic processes that shape inflammatory signaling and cellular differentiation. Altered sterol sulfation dynamics are relevant to studies of metabolic dysfunction, atherosclerosis-related mechanisms, and tissue remodeling without implying clinical outcomes.

SULT2B1 CRISPR Activation Plasmid (m) provides a targeted, non-destructive approach to upregulating endogenous Sult2b1 expression without altering the underlying DNA sequence.

SULT2B1 CRISPR Activation Plasmid (m) is a three-plasmid synergistic activation mediator (SAM) system engineered for highly efficient, site-specific transcriptional upregulation of the Sult2b1 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 Sult2b1 transcriptional start site, where VP64, p65, and HSF1 act in concert to recruit transcriptional machinery and drive upregulation of endogenous SULT2B1 expression. Unlike nuclease-active Cas9, dCas9 does not introduce double-strand breaks or modify the genomic sequence, preserving the native Sult2b1 locus and enabling the study of SULT2B1-dependent transcriptional responses at the endogenous locus, making it a valuable tool for functional studies, target gene identification, and the modeling of SULT2B1 pathway restoration in tumor cells with silenced or reduced Sult2b1 expression.

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