V-ATPase G1 Lentiviral Activation Particles (h): sc-406125-LAC
- Target species: human
- 200 µl of transduction-ready, high-titer CRISPR/dCas9 Lentiviral Activation Particles
- V-ATPase G1 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
- V-ATPase G1 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 V-ATPase G1 Lentiviral Activation Plasmid (h) and V-ATPase G1 Lentiviral Activation Plasmid (h2) target distinct regulatory regions of the ATP6V1G1 promoter. One or both designs may be available
- Following transfection, gene activation efficiency can be assayed by WB, IF or IHC using antibody: V-ATPase G1 Antibody (D-5): sc-25333
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
V-ATPase G1 Lentiviral Activation Particles (h) | sc-406125-LAC | 200 µl | $455.00 | |||
V-ATPase G1 Lentiviral Activation Particles (h2) | sc-406125-LAC-2 | 200 µl | $455.00 |
ATP6V1G1 encodes the G1 subunit of the vacuolar H+-ATPase (V-ATPase) V1 domain, a multi-subunit proton pump that drives ATP-dependent acidification of endosomes, lysosomes, and secretory vesicles. By regulating luminal pH, V-ATPase activity supports receptor-mediated endocytosis, vesicular trafficking, autophagic flux, and lysosomal enzyme activation, and it contributes to cellular pH homeostasis. Perturbation of V-ATPase subunit composition or activity is linked to altered nutrient sensing and mTOR-associated signaling, defective protein turnover, and stress responses. Dysregulated organellar acidification and endolysosomal function are recurrent features across cancer cell biology and neurodegeneration research, making ATP6V1G1 a useful target for mechanistic studies of vesicle biology.
V-ATPase G1 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 ATP6V1G1 upregulation across a broader range of human cell types.
V-ATPase G1 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 ATP6V1G1 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous V-ATPase G1 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native ATP6V1G1 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.