Hepatic Lipase CRISPR Activation Plasmid (h): sc-403928-ACT

LIPC encodes hepatic lipase, a liver- and endothelium-associated lipolytic enzyme that hydrolyzes triglycerides and phospholipids in circulating lipoproteins, thereby remodeling HDL and apoB-containing particles. Through its actions at the hepatocyte surface and within the vascular compartment, hepatic lipase contributes to lipoprotein uptake, reverse cholesterol transport, and broader lipid homeostasis. Variation in LIPC expression or activity has been linked to altered plasma lipid profiles, including changes in HDL cholesterol and triglyceride-rich lipoproteins, connecting this pathway to cardiometabolic phenotypes. As a nodal regulator of lipoprotein metabolism, LIPC is frequently studied in hepatocyte biology, lipid trafficking, and nutrient-responsive transcriptional networks.

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

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

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