TRB-3 Lentiviral Activation Particles (m): sc-432803-LAC

Mouse Trib3 encodes TRB-3, a catalytically inactive pseudokinase that functions as a stress-inducible scaffold modulating intracellular signaling. TRB-3 is commonly linked to insulin/IGF–PI3K–AKT pathway regulation through protein–protein interactions, shaping downstream effects on glucose metabolism, cell survival, autophagy, and transcriptional programs during ER stress and nutrient deprivation. It also interfaces with inflammatory and stress-response networks, including ATF4/CHOP-driven unfolded protein response signaling and context-dependent MAPK and NF-κB activity. Altered TRB-3 expression has been associated with metabolic dysregulation, fibrosis and inflammation-related processes, and tumor-adaptive stress phenotypes, making Trib3 a relevant target for mechanistic studies in cardiometabolic and cancer biology models.

TRB-3 Lentiviral Activation Particles (m) address this need by packaging the complete synergistic activation mediator (SAM) transcriptional activation system into transduction-ready, high-titer lentiviral particles, enabling efficient Trib3 upregulation across a broader range of human cell types.

TRB-3 Lentiviral Activation Particles (m) 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 Trib3 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous TRB-3 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native Trib3 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.