FGF-10 Lentiviral Activation Particles (h): sc-417825-LAC

FGF10 encodes fibroblast growth factor 10 (FGF-10), a secreted ligand that preferentially signals through FGFR2b to regulate epithelial–mesenchymal communication, cell proliferation, migration, and tissue patterning. FGF-10 activates canonical receptor tyrosine kinase cascades including MAPK/ERK, PI3K–AKT, and PLCγ signaling, influencing morphogenesis, wound-associated remodeling, and stromal–epithelial crosstalk. Dysregulated FGF10/FGFR2b signaling has been implicated in aberrant developmental programs and disease-associated changes in tissue architecture, including contexts of fibrosis and tumor microenvironment remodeling. As a pathway node with strong paracrine effects, FGF10 is frequently studied to dissect growth factor–driven transcriptional programs and epithelial lineage behaviors.

FGF-10 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 FGF10 upregulation across a broader range of human cell types.

FGF-10 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 FGF10 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous FGF-10 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native FGF10 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.