Met Lentiviral Activation Particles (h): sc-400101-LAC

Human MET encodes the Met receptor tyrosine kinase, the high-affinity receptor for hepatocyte growth factor (HGF). Upon ligand binding, Met undergoes autophosphorylation and activates downstream signaling through PI3K–AKT, RAS–MAPK, STAT, and SRC/FAK pathways to regulate proliferation, survival, motility, epithelial–mesenchymal transitions, and tissue morphogenesis. MET dysregulation via amplification, overexpression, mutation, or aberrant HGF stimulation is linked to invasive growth programs and altered cell–microenvironment interactions relevant to oncology and developmental biology. In vitro, MET signaling is frequently studied for its roles in migration, angiogenic signaling, and resistance-associated network rewiring.

Met 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 MET upregulation across a broader range of human cell types.

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