DC-SIGN Lentiviral Activation Particles (h): sc-401368-LAC

CD209 encodes DC-SIGN (dendritic cell-specific intercellular adhesion molecule-3-grabbing non-integrin), a C-type lectin receptor prominently expressed on dendritic cells and select macrophage populations that recognizes high-mannose and fucosylated glycans. Through ligand binding, DC-SIGN influences pathogen recognition, antigen uptake, endosomal trafficking, and immune synapse formation, while coupling to signaling programs involving Raf-1–dependent modulation of NF-κB and broader innate immune transcriptional responses. This receptor participates in crosstalk with Toll-like receptor pathways and shapes cytokine output that can bias downstream T cell priming and polarization. Dysregulated DC-SIGN activity and expression patterns have been linked to altered host–pathogen interactions and immune microenvironment remodeling in infectious disease models and inflammatory contexts.

DC-SIGN 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 CD209 upregulation across a broader range of human cell types.

DC-SIGN 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 CD209 transcriptional start site, where VP64, p65, and HSF1 act cooperatively to recruit endogenous transcriptional machinery and drive sustained upregulation of endogenous DC-SIGN expression. The use of nuclease-inactive dCas9 avoids the introduction of double-strand DNA breaks and preserves the native CD209 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.