PPP1R12C Lentiviral Activation Particles (h): sc-412332-LAC

PPP1R12C encodes the myosin phosphatase targeting subunit 3 (MYPT3), a regulatory component of protein phosphatase 1 that helps direct PP1 catalytic activity toward cytoskeletal substrates. Through controlling phosphorylation states of myosin light chain and related actomyosin regulators, PPP1R12C contributes to cell contractility, adhesion dynamics, and motility, integrating signaling inputs from RhoA/ROCK and other kinase pathways. Altered PP1 targeting and myosin phosphatase function can perturb cytoskeletal remodeling and mechanotransduction, processes frequently implicated in tumor cell invasion, fibrosis-associated remodeling, and vascular smooth muscle dysfunction. PPP1R12C expression and phosphorylation-dependent regulation are therefore relevant for studies of stress fiber organization, cell shape control, and signaling crosstalk that tunes contractile phenotypes.

PPP1R12C 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 PPP1R12C upregulation across a broader range of human cell types.

PPP1R12C 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 PPP1R12C transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous PPP1R12C expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native PPP1R12C 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.