TTP Lentiviral Activation Particles (h): sc-400722-LAC

Human ZFP36 encodes tristetraprolin (TTP), an AU-rich element–binding RNA-binding protein that promotes rapid mRNA deadenylation and decay to limit expression of inflammatory mediators and immediate-early genes. TTP recruits CCR4–NOT and related decay machinery to regulate transcript turnover, shaping innate immune signaling, stress responses, and feedback control of cytokine pathways such as TNF/NF-κB and MAPK. Dysregulated ZFP36/TTP activity is associated with aberrant cytokine production and chronic inflammation, and altered expression has been reported across immune dysregulation contexts and cancer-related phenotypes linked to post-transcriptional control. As a node in mRNA stability networks, ZFP36 is widely used to interrogate RNA decay, macrophage activation programs, and signaling-dependent transcriptome remodeling.

TTP 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 ZFP36 upregulation across a broader range of human cell types.

TTP 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 ZFP36 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous TTP expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native ZFP36 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.