TSPAN7 Lentiviral Activation Particles (h): sc-404065-LAC

TSPAN7 (tetraspanin-7) is a four-pass transmembrane tetraspanin that organizes tetraspanin-enriched microdomains and modulates cell-surface receptor trafficking, adhesion, and actin-associated membrane dynamics. In neural and epithelial contexts, it contributes to cytoskeletal remodeling and synaptic or junctional architecture through interactions with partner membrane proteins, influencing signaling nodes downstream of receptor clustering and endocytosis. Altered TSPAN7 expression or function has been linked to neurodevelopmental phenotypes and synaptic dysfunction, supporting its relevance to studies of neuronal connectivity and plasticity. Because tetraspanins tune membrane compartmentalization rather than acting as classical enzymes, TSPAN7 is frequently investigated for its effects on pathway crosstalk and cell-state transitions.

TSPAN7 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 TSPAN7 upregulation across a broader range of human cell types.

TSPAN7 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 TSPAN7 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous TSPAN7 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native TSPAN7 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.