ACADVL (VLCAD) Lentiviral Activation Particles (h): sc-403111-LAC
- Target species: human
- 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
- ACADVL 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
- ACADVL 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 ACADVL Lentiviral Activation Plasmid (h) and ACADVL Lentiviral Activation Plasmid (h2) target distinct regulatory regions of the ACADVL promoter. One or both designs may be available
- Following transfection, gene activation efficiency can be assayed by WB, IF or IHC using antibody: ACADVL Antibody (H-7): sc-376239
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
ACADVL (VLCAD) Lentiviral Activation Particles (h) | sc-403111-LAC | 200 µl | $455.00 | |||
ACADVL (VLCAD) Lentiviral Activation Particles (h2) | sc-403111-LAC-2 | 200 µl | $455.00 |
ACADVL encodes very long-chain acyl-CoA dehydrogenase (VLCAD), a mitochondrial flavoprotein that catalyzes the first dehydrogenation step in β-oxidation of long-chain fatty acyl-CoAs. VLCAD supports energy production from fatty acids, contributing to mitochondrial redox balance and metabolic flexibility in tissues with high oxidative demand such as heart and skeletal muscle. Disruption or reduced activity of ACADVL is linked to impaired long-chain fatty acid oxidation, altered acylcarnitine profiles, and mitochondrial stress responses. These metabolic defects are studied in the context of inherited fatty acid oxidation disorders and broader research into cardiometabolic dysfunction and mitochondrial disease mechanisms.
ACADVL 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 ACADVL upregulation across a broader range of human cell types.
ACADVL 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 ACADVL transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous ACADVL expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native ACADVL 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.