EGFL6 Lentiviral Activation Particles (h): sc-411850-LAC

EGFL6 encodes an extracellular matrix–associated secreted protein belonging to the EGF-like family that contributes to cell–matrix interactions and microenvironmental signaling. EGFL6 has been linked to regulation of endothelial and epithelial cell behavior, including migration, adhesion, and survival, consistent with roles in tissue remodeling and angiogenesis-associated processes. Through its EGF-like domains, EGFL6 can modulate signaling networks that intersect with integrin-mediated pathways and growth factor–responsive programs influencing cytoskeletal dynamics. Dysregulated EGFL6 expression has been reported in multiple disease contexts, supporting its use as a molecular handle to study vascular remodeling, tumor microenvironment biology, and cell motility phenotypes in human model systems.

EGFL6 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 EGFL6 upregulation across a broader range of human cell types.

EGFL6 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 EGFL6 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous EGFL6 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native EGFL6 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.