RKIP Lentiviral Activation Particles (h): sc-401270-LAC

Human PEBP1 encodes Raf kinase inhibitory protein (RKIP), a conserved modulator of intracellular signal transduction that restrains MAPK/ERK signaling by interfering with RAF–MEK interactions and also influences GPCR pathways through regulation of GRK2. RKIP contributes to the balance between proliferation, differentiation, apoptosis, and stress responses, and it can shape pathway crosstalk involving NF-κB and other transcriptional programs. Altered RKIP expression has been associated with changes in cellular motility, invasion-related phenotypes, and inflammatory signaling states across diverse disease models. As a nodal signaling regulator, PEBP1 is frequently investigated in studies of kinase network rewiring, feedback control, and context-dependent transcriptional outputs.

RKIP 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 PEBP1 upregulation across a broader range of human cell types.

RKIP 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 PEBP1 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous RKIP expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native PEBP1 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.