BCKDE1A Lentiviral Activation Particles (h): sc-417950-LAC
- Target species: human
- 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
- BCKDE1A 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
- BCKDE1A 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 BCKDE1A Lentiviral Activation Plasmid (h) and BCKDE1A Lentiviral Activation Plasmid (h2) target distinct regulatory regions of the BCKDHA promoter. One or both designs may be available
- Following transfection, gene activation efficiency can be assayed by WB, IF or IHC using antibody: BCKDE1A Antibody (H-5): sc-271538
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
BCKDE1A Lentiviral Activation Particles (h) | sc-417950-LAC | 200 µl | $455.00 |
BCKDHA encodes the E1α subunit of the mitochondrial branched-chain α-ketoacid dehydrogenase (BCKDH) complex, a key enzymatic node in oxidative catabolism of the branched-chain amino acids leucine, isoleucine, and valine. Within the mitochondrial matrix, BCKDH links amino acid turnover to central carbon metabolism by generating acyl-CoA derivatives that feed downstream energy-producing pathways and support metabolic homeostasis. BCKDHA function integrates with cofactor-dependent oxidative decarboxylation processes and mitochondrial quality control, making it a useful entry point for studies of nutrient sensing and mitochondrial metabolism. Disruption or dysregulation of BCKDHA is associated with impaired branched-chain amino acid metabolism and is relevant to inborn errors of metabolism such as maple syrup urine disease.
BCKDE1A 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 BCKDHA upregulation across a broader range of human cell types.
BCKDE1A 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 BCKDHA transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous BCKDE1A expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native BCKDHA 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.