caveolin-3 Lentiviral Activation Particles (h): sc-400569-LAC

CAV3 encodes caveolin-3, a muscle-enriched integral membrane protein that scaffolds caveolae and organizes signaling microdomains at the sarcolemma. Caveolin-3 regulates membrane trafficking, mechanotransduction, and lipid homeostasis, and it modulates pathways including insulin receptor/PI3K–AKT signaling, nitric oxide signaling, and ion channel localization. Through interactions with the dystrophin–glycoprotein complex and cytoskeletal elements, caveolin-3 supports membrane stability during contraction and contributes to excitation–contraction coupling. Dysregulation or mutation of CAV3 is associated with skeletal muscle and cardiac phenotypes, making it a relevant target for studying caveolae biology, sarcolemmal integrity, and stress-response signaling in human cells.

caveolin-3 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 CAV3 upregulation across a broader range of human cell types.

caveolin-3 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 CAV3 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous caveolin-3 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native CAV3 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.