ADAM9 Lentiviral Activation Particles (h): sc-403665-LAC

ADAM9 encodes a transmembrane metalloprotease–disintegrin that mediates ectodomain shedding of diverse cell-surface proteins, shaping extracellular matrix remodeling, cell–cell adhesion, and receptor/ligand availability. Through proteolytic processing of substrates involved in growth factor and cytokine signaling, ADAM9 can influence pathways linked to epithelial–mesenchymal dynamics, migration, and inflammatory responses. Its activity intersects with integrin-dependent adhesion and metalloprotease networks that regulate membrane protein turnover and pericellular proteolysis. Dysregulated ADAM9 expression or activity has been associated with tumor invasion biology, fibrosis-related remodeling, and neuroinflammatory processes, making it a useful target for mechanistic studies of protease-driven signaling.

ADAM9 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 ADAM9 upregulation across a broader range of human cell types.

ADAM9 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 ADAM9 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous ADAM9 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native ADAM9 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.