ATP6V0E1 Lentiviral Activation Particles (h): sc-411234-LAC

ATP6V0E1 encodes the V-ATPase V0 subunit E1, a core component of the vacuolar H\+-ATPase that couples ATP hydrolysis to proton translocation across endomembrane systems. By acidifying endosomes, lysosomes, and secretory vesicles, ATP6V0E1 supports receptor-mediated endocytosis, lysosomal hydrolase activity, protein turnover, and autophagy, and it contributes to pH-dependent trafficking within the Golgi–endosomal network. V-ATPase function also interfaces with nutrient-sensing and proteostasis pathways, including mTORC1 regulation at the lysosomal surface and stress responses linked to organellar acid-base balance. Dysregulated vesicular acidification and V-ATPase subunit perturbations are associated with cellular phenotypes relevant to neurodegeneration, cancer cell metabolism and invasion, and immune signaling that depends on endolysosomal processing.

ATP6V0E1 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 ATP6V0E1 upregulation across a broader range of human cell types.

ATP6V0E1 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 ATP6V0E1 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous ATP6V0E1 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native ATP6V0E1 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.