IGF2BP3 Lentiviral Activation Particles (h): sc-402603-LAC

IGF2BP3 (insulin-like growth factor 2 mRNA-binding protein 3) is an oncofetal RNA-binding protein that regulates post-transcriptional gene expression by binding and stabilizing target mRNAs and modulating their localization and translation. It participates in RNA granule dynamics and influences pathways governing cell-cycle progression, migration, and stress responses, in part through control of transcripts involved in PI3K–AKT and MAPK signaling outputs. IGF2BP3 expression is low in most adult tissues but is frequently upregulated in multiple tumor types, where it associates with aggressive phenotypes and altered differentiation programs. As a result, IGF2BP3 is widely studied as a mechanistic node linking mRNA fate determination to proliferative and invasive cellular states.

IGF2BP3 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 IGF2BP3 upregulation across a broader range of human cell types.

IGF2BP3 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 IGF2BP3 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous IGF2BP3 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native IGF2BP3 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.