Perlecan Lentiviral Activation Particles (m): sc-420986-LAC

Mouse Hspg2 encodes perlecan, a large heparan sulfate proteoglycan of basement membranes and pericellular matrices that scaffolds extracellular matrix organization and regulates the bioavailability of growth factors. Perlecan modulates cell adhesion, migration, and mechanotransduction by coordinating signaling through pathways such as FGF, VEGF, PDGF, and TGF-β and by shaping integrin-dependent interactions with laminins and collagens. In vascular, skeletal, and neural tissues, Hspg2 helps maintain basement membrane integrity and influences angiogenesis and tissue remodeling. Dysregulated perlecan expression or matrix deposition is implicated in fibrosis, tumor–stroma interactions, and developmental defects, making it a key target for studying extracellular matrix signaling networks in mouse models.

Perlecan Lentiviral Activation Particles (m) address this need by packaging the complete synergistic activation mediator (SAM) transcriptional activation system into transduction-ready, high-titer lentiviral particles, enabling efficient Hspg2 upregulation across a broader range of human cell types.

Perlecan Lentiviral Activation Particles (m) 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 Hspg2 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous Perlecan expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native Hspg2 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.