SVEP1 Lentiviral Activation Particles (h): sc-413315-LAC

SVEP1 (sushi, von Willebrand factor type A, EGF and pentraxin domain containing 1) encodes a large extracellular matrix–associated protein that supports cell–cell and cell–matrix adhesion and contributes to tissue organization. SVEP1 engages integrin-dependent signaling and is linked to regulation of vascular and lymphatic remodeling, inflammatory cell recruitment, and stromal–epithelial interactions that shape developmental and repair programs. Altered SVEP1 expression has been associated with cardiometabolic and vascular traits, fibrotic remodeling, and tumor microenvironment features, making it a useful target for dissecting extracellular matrix–driven signaling networks. Functional studies commonly examine SVEP1 in endothelial and mesenchymal contexts to understand how matrix cues modulate migration, differentiation, and immune–stromal crosstalk.

SVEP1 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 SVEP1 upregulation across a broader range of human cell types.

SVEP1 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 SVEP1 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous SVEP1 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native SVEP1 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.