Not CRISPR data: the image illustrates antibody quality for visualizing CRISPR experiment results.
Not CRISPR data: the image illustrates antibody quality for visualizing CRISPR experiment results.
ChREBP Lentiviral Activation Particles (h): sc-401803-LAC
- Target species: human
- 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
- ChREBP Lentiviral Activation Particles (h) is a synergistic activation mediator (SAM) transcription activation system designed to specifically and efficiently upregulate gene expression via lentiviral transduction of cells
- ChREBP Lentiviral Activation Particles (h) contain the following SAM Activation elements: a deactivated Cas9 (dCas9) nuclease (D10A and N863A) fused to the transactivation domain VP64, an MS2-p65-HSF1 fusion protein and a target-specific 20 nt guide RNA. They also contain the blasticidin, hygromycin and puromycin resistance genes
- Upon transduction, the SAM complex binds to a site-specific region approximately 200-250 nt upstream of the transcriptional start site and provides robust recruitment of transcription factors for highly efficient gene activation
- gRNAs encoded by ChREBP Lentiviral Activation Plasmid (h) and ChREBP Lentiviral Activation Plasmid (h2) target distinct regulatory regions of the MLXIPL promoter. One or both designs may be available
- Following transfection, gene activation efficiency can be assayed by WB, IF or IHC using antibody: ChREBP Antibody (G-12): sc-515922
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
ChREBP Lentiviral Activation Particles (h) | sc-401803-LAC | 200 µl | $455.00 |
MLXIPL encodes carbohydrate-responsive element-binding protein (ChREBP), a glucose-sensing transcription factor that couples intracellular carbohydrate flux to gene programs controlling glycolysis, de novo lipogenesis, and triglyceride synthesis. In response to carbohydrate metabolites, ChREBP translocates to the nucleus and binds carbohydrate response elements to regulate metabolic enzymes and transporters, integrating nutrient status with hepatic and adipose energy storage pathways. This regulatory axis intersects with insulin signaling, AMP-activated protein kinase (AMPK) modulation, and broader transcriptional networks governing lipid homeostasis. Dysregulated ChREBP activity has been associated with metabolic phenotypes relevant to hepatic steatosis, insulin resistance, and cardiometabolic risk, making MLXIPL a useful node for mechanistic studies of nutrient-driven gene regulation.
ChREBP Lentiviral Activation Particles (h) address this need by packaging the complete synergistic activation mediator (SAM) transcriptional activation system into transduction-ready, high-titer lentiviral particles, enabling efficient MLXIPL upregulation across a broader range of human cell types.
ChREBP Lentiviral Activation Particles (h) deliver all functional components of the synergistic activation mediator (SAM) system via lentiviral transduction. The system comprises three particle preparations co-transduced into target cells: one encoding catalytically inactive dCas9 (D10A and N863A mutations) fused to the VP64 transactivation domain with a blasticidin resistance gene; one encoding the MS2-p65-HSF1 fusion protein with a hygromycin resistance gene; and one encoding a target-specific 20 nt sgRNA fused to two MS2 RNA aptamers with a puromycin resistance gene. Following lentiviral transduction and genomic integration of the expression cassettes, the SAM components are stably expressed and assemble at the target locus within the proximal promoter region upstream of the MLXIPL transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous ChREBP expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native MLXIPL genomic locus and regulatory architecture.
The lentiviral format offers several practical advantages: stable genomic integration supports heritable activation across cell divisions; high-titer particle preparations eliminate the need for in-house viral production; and compatibility with primary, non-dividing, and transfection-resistant cell types expands experimental accessibility. Successful transduction can be confirmed and enriched through triple antibiotic selection using puromycin, hygromycin, and blasticidin.
For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.