eIF4B Lentiviral Activation Particles (h): sc-402494-LAC

EIF4B encodes the human translation initiation factor eIF4B, a regulator of cap-dependent mRNA translation that promotes 43S preinitiation complex recruitment and enhances RNA helicase activity within the eIF4F axis, facilitating scanning through structured 5′ UTRs. Through modulation of translation efficiency, eIF4B integrates signaling from growth and stress pathways, including PI3K–AKT–mTOR and MAPK, to shape proteome output during proliferation and cellular adaptation. Dysregulated eIF4B activity has been associated with altered translational control programs implicated in oncogenic signaling and survival phenotypes, and it is frequently studied as a node linking upstream kinase networks to selective mRNA translation. These features make EIF4B a useful target for dissecting translational regulation, signaling-to-translation coupling, and pathway-dependent proteostasis in human cells.

eIF4B 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 EIF4B upregulation across a broader range of human cell types.

eIF4B 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 EIF4B transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous eIF4B expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native EIF4B 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.