ADAM15 Lentiviral Activation Particles (h): sc-405627-LAC

ADAM15 encodes a membrane-anchored metalloprotease-disintegrin that modulates cell–cell and cell–matrix interactions through proteolytic shedding and integrin engagement. ADAM15 activity influences signaling networks linked to adhesion and motility, including focal adhesion dynamics, cytoskeletal remodeling, and growth factor receptor pathway tuning via ectodomain processing of surface proteins. It is expressed in multiple tissues and has been studied in contexts of inflammation, vascular biology, and tumor cell invasion where altered protease activity and adhesion signaling contribute to disease-associated phenotypes. These properties make ADAM15 a useful node for dissecting protease-dependent regulation of migration, barrier function, and microenvironmental interactions in human cell models.

ADAM15 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 ADAM15 upregulation across a broader range of human cell types.

ADAM15 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 ADAM15 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous ADAM15 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native ADAM15 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.