17β-HSD13 CRISPR Activation Plasmid (h): sc-415608-ACT

HSD17B13 encodes 17β-HSD13, a liver-enriched member of the hydroxysteroid 17β-dehydrogenase family implicated in cellular lipid metabolism and redox-dependent steroid/retinoid processing. The protein localizes predominantly to hepatocyte lipid droplets and is linked to regulation of lipid droplet homeostasis, fatty acid handling, and metabolic stress responses within hepatic pathways. Genetic and expression studies associate HSD17B13 with susceptibility and progression of liver disease phenotypes, including steatosis-related injury and inflammatory liver conditions. As a result, HSD17B13 serves as a functional entry point for mechanistic studies connecting hepatic metabolism, lipid storage dynamics, and liver pathology-relevant cellular states.

17β-HSD13 CRISPR Activation Plasmid (h) provides a targeted, non-destructive approach to upregulating endogenous HSD17B13 expression without altering the underlying DNA sequence.

17β-HSD13 CRISPR Activation Plasmid (h) is a three-plasmid synergistic activation mediator (SAM) system engineered for highly efficient, site-specific transcriptional upregulation of the HSD17B13 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 HSD17B13 transcriptional start site, where VP64, p65, and HSF1 act in concert to recruit transcriptional machinery and drive upregulation of endogenous 17β-HSD13 expression. Unlike nuclease-active Cas9, dCas9 does not introduce double-strand breaks or modify the genomic sequence, preserving the native HSD17B13 locus and enabling the study of 17β-HSD13-dependent transcriptional responses at the endogenous locus, making it a valuable tool for functional studies, target gene identification, and the modeling of 17β-HSD13 pathway restoration in tumor cells with silenced or reduced HSD17B13 expression.

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