Matriptase Lentiviral Activation Particles (h): sc-402971-LAC

Human ST14 encodes matriptase, a type II transmembrane serine protease that regulates pericellular proteolysis at the cell surface. Matriptase participates in epithelial barrier homeostasis and remodeling by activating substrates such as pro-hepatocyte growth factor and protease-activated receptor signaling, and by processing extracellular matrix–associated proteins. Through these activities it influences cell adhesion, migration, and epithelial differentiation programs, with relevance to dysregulated protease networks observed in epithelial inflammation and cancer biology. ST14 function is frequently studied in the context of protease–inhibitor balance, membrane-anchored proteolytic cascades, and epithelial tissue integrity.

Matriptase 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 ST14 upregulation across a broader range of human cell types.

Matriptase 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 ST14 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous Matriptase expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native ST14 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.