TLR4 Lentiviral Activation Particles (h): sc-400068-LAC

Human TLR4 (Toll-like receptor 4) is a pattern-recognition receptor that detects lipopolysaccharide and related microbial or damage-associated ligands to initiate innate immune signaling. Upon activation, TLR4 engages MYD88- and TRIF-dependent pathways, driving NF-κB, MAPK, and IRF3 programs that regulate pro-inflammatory cytokines and type I interferon responses. TLR4 signaling influences myeloid activation, antigen presentation, and tissue inflammatory tone, linking it to host defense as well as dysregulated inflammation. Altered TLR4 activity and downstream transcriptional outputs are frequently studied in sepsis biology, chronic inflammatory disease mechanisms, metabolic inflammation, and tumor–immune microenvironment research.

TLR4 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 TLR4 upregulation across a broader range of human cell types.

TLR4 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 TLR4 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous TLR4 expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native TLR4 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.