Fibronectin Lentiviral Activation Particles (h): sc-400082-LAC

FN1 encodes fibronectin, a high-molecular-weight extracellular matrix glycoprotein that assembles into fibrillar networks and mediates cell adhesion, migration, and mechanotransduction through integrin engagement. Fibronectin coordinates extracellular matrix organization, focal adhesion dynamics, and cytoskeletal remodeling, influencing pathways such as integrin–FAK/SRC signaling, Rho GTPase regulation, and TGF-β–associated matrix remodeling. As a central component of wound repair and tissue homeostasis, fibronectin contributes to epithelial–mesenchymal transition, angiogenic programs, and stromal interactions. Dysregulated FN1 expression and altered fibronectin matrix deposition are implicated in fibrotic remodeling, inflammatory microenvironments, and tumor–stroma crosstalk relevant to metastasis-associated phenotypes.

Fibronectin 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 FN1 upregulation across a broader range of human cell types.

Fibronectin 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 FN1 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous Fibronectin expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native FN1 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.