IGFBP3 Lentiviral Activation Particles (h): sc-400682-LAC

IGFBP3 (insulin-like growth factor binding protein 3) is a secreted regulatory protein that binds IGF-I and IGF-II with high affinity to modulate IGF bioavailability, receptor engagement, and downstream PI3K–AKT and MAPK signaling. Beyond IGF sequestration, IGFBP3 participates in cell cycle control, apoptosis, senescence, and stress responses through context-dependent interactions with extracellular matrix components and cell-surface or nuclear partners. Its expression is dynamically regulated by hormonal and inflammatory cues and is frequently altered in cancer biology, metabolic dysregulation, and tissue remodeling settings. These properties make IGFBP3 a useful node for dissecting growth factor signaling, proliferative control, and microenvironment-dependent phenotypes in human cells.

IGFBP3 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 IGFBP3 upregulation across a broader range of human cell types.

IGFBP3 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 IGFBP3 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous IGFBP3 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native IGFBP3 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.