CPI-17 Lentiviral Activation Particles (h): sc-401966-LAC

PPP1R14A encodes CPI-17, a phosphorylation-dependent inhibitor of myosin light chain phosphatase (MLCP/PP1) that amplifies contractile signaling by sustaining myosin regulatory light chain phosphorylation. Upon activation by PKC and RhoA/ROCK-linked inputs, CPI-17 integrates Ca²⁺ sensitization pathways to modulate smooth muscle tone, cytoskeletal tension, and actomyosin dynamics. This regulatory node influences GPCR-driven contractility, cell migration, and barrier properties across vascular and visceral tissues. Dysregulated PPP1R14A/CPI-17 signaling has been associated with altered smooth muscle hypercontractility and remodeling processes relevant to cardiovascular and airway disease biology, supporting its use as a mechanistic handle in signaling and tissue physiology studies.

CPI-17 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 PPP1R14A upregulation across a broader range of human cell types.

CPI-17 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 PPP1R14A transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous CPI-17 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native PPP1R14A 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.