G3BP2 Lentiviral Activation Particles (h): sc-403630-LAC

G3BP2 (G3BP stress granule assembly factor 2) is an RNA-binding protein that functions as a central scaffold for stress granule nucleation and mRNA triage, coordinating transcript stability and translation during cellular stress. It participates in post-transcriptional regulatory networks linked to interferon signaling, innate immune responses, and adaptation to oxidative and endoplasmic reticulum stress, with downstream impacts on cell cycle progression and survival pathways. Through interactions with signaling and RNA metabolism components, G3BP2 helps couple environmental cues to ribonucleoprotein remodeling and translational control. Dysregulation of stress granule dynamics and RNA homeostasis involving G3BP2 has been associated with disease-relevant processes including tumor cell stress tolerance, neurodegeneration-related protein/RNA aggregation, and inflammatory signaling.

G3BP2 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 G3BP2 upregulation across a broader range of human cell types.

G3BP2 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 G3BP2 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous G3BP2 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native G3BP2 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.