SPA-L3 Lentiviral Activation Particles (h): sc-411666-LAC

SIPA1L3 encodes signal-induced proliferation-associated 1-like protein 3 (SPA-L3), a Rap/Ras pathway–associated scaffold that links small GTPase signaling to cytoskeletal remodeling and cell adhesion programs. Through its modular interaction domains, SPA-L3 is implicated in coordinating actin dynamics, membrane trafficking, and junctional organization, processes that shape cell polarity and tissue architecture. Dysregulated Rap/Ras signaling and altered cytoskeletal control are recurring features in tumor progression and invasive phenotypes, making SIPA1L3 a useful node for studying signaling-to-structure coupling. In the nervous system, related signaling frameworks support neurite outgrowth and synaptic organization, providing additional context for investigating developmental and neurobiological mechanisms.

SPA-L3 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 SIPA1L3 upregulation across a broader range of human cell types.

SPA-L3 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 SIPA1L3 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous SPA-L3 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native SIPA1L3 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.