IGFBP2 Lentiviral Activation Particles (m): sc-421063-LAC

Igfbp2 encodes insulin-like growth factor binding protein 2 (IGFBP2), a secreted regulator of IGF bioavailability that modulates IGF1/IGF2 signaling strength, receptor engagement, and downstream PI3K–AKT and MAPK pathway activity. By buffering and localizing IGF ligands in the extracellular milieu, IGFBP2 influences cell proliferation, survival, migration, and matrix interactions, and can shape tissue growth and metabolic homeostasis. In mouse models, altered Igfbp2 expression has been linked to changes in adiposity and insulin sensitivity as well as context-dependent effects on inflammation and tissue remodeling. These properties make Igfbp2 a useful target for studying growth factor signaling dynamics, tumor microenvironment biology, and endocrine–paracrine crosstalk in development and disease-relevant states.

IGFBP2 Lentiviral Activation Particles (m) address this need by packaging the complete synergistic activation mediator (SAM) transcriptional activation system into transduction-ready, high-titer lentiviral particles, enabling efficient Igfbp2 upregulation across a broader range of human cell types.

IGFBP2 Lentiviral Activation Particles (m) 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 Igfbp2 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous IGFBP2 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native Igfbp2 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.