G3BP1 Lentiviral Activation Particles (h): sc-400745-LAC

G3BP1 (Ras GTPase-activating protein-binding protein 1) is an RNA-binding protein that functions as a central nucleator of cytoplasmic stress granules, coordinating mRNA triage, translation repression, and RNA stability during cellular stress. Through its RRM and RGG domains, G3BP1 integrates signaling and RNA metabolism by engaging pathways linked to antiviral innate immune responses, MAPK/ERK signaling, and RNP remodeling. It also interfaces with DNA damage and replication stress programs via regulation of transcript fate and protein-protein interaction networks that shape cell survival decisions. Dysregulated G3BP1 activity has been associated with aberrant stress granule dynamics and altered RNA regulatory circuits observed across cancer biology, neurodegeneration, and virus–host interactions, making it a useful node for mechanistic studies of stress-adaptive phenotypes.

G3BP1 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 G3BP1 upregulation across a broader range of human cell types.

G3BP1 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 G3BP1 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous G3BP1 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native G3BP1 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.