IGF-1 Receptor α/β/IGF1R Lentiviral Activation Particles (h): sc-400084-LAC

IGF1R encodes the insulin-like growth factor 1 receptor (IGF-1 Receptor α/β), a receptor tyrosine kinase that binds IGF-1/IGF-2 to regulate cell growth, survival, and metabolism. Ligand-induced autophosphorylation activates downstream PI3K–AKT–mTOR and RAS–RAF–MEK–ERK signaling, integrating mitogenic and anti-apoptotic cues with cellular bioenergetics. IGF1R signaling influences differentiation, cell-cycle progression, and stress responses through adaptor proteins such as IRS1/2 and SHC. Dysregulated IGF1R activity is associated with aberrant proliferative signaling and altered metabolic programs observed across diverse oncology and metabolic disease research contexts.

IGF-1 Receptor α/β/IGF1R 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 IGF1R upregulation across a broader range of human cell types.

IGF-1 Receptor α/β/IGF1R 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 IGF1R transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous IGF-1 Receptor α/β/IGF1R expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native IGF1R 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.