FGF-7 Lentiviral Activation Particles (h2): sc-401243-LAC-2

Human FGF7 encodes fibroblast growth factor 7 (FGF-7, also known as keratinocyte growth factor), a paracrine ligand produced primarily by mesenchymal cells that activates FGFR2b to promote epithelial cell proliferation, migration, and differentiation. FGF-7 signaling engages canonical receptor tyrosine kinase pathways including MAPK/ERK and PI3K/AKT, contributing to epithelial–stromal crosstalk, tissue repair programs, and regulation of barrier-forming epithelia. Dysregulated FGF7/FGFR2b activity has been implicated in aberrant epithelial growth and remodeling observed in cancers and inflammatory or fibrotic conditions, supporting its use as a mechanistic node in disease biology studies. Gene editing of FGF7 enables functional interrogation of ligand-dependent receptor signaling, modeling of microenvironment-driven phenotypes in organoids and co-culture systems, and validation of pathway biomarkers in human cell contexts.

FGF-7 Lentiviral Activation Particles (h2) address this need by packaging the complete synergistic activation mediator (SAM) transcriptional activation system into transduction-ready, high-titer lentiviral particles, enabling efficient FGF7 upregulation across a broader range of human cell types.

FGF-7 Lentiviral Activation Particles (h2) 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 FGF7 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous FGF-7 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native FGF7 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.