DC-SIGN CRISPR Activation Plasmid (h): sc-401368-ACT

CD209 encodes DC-SIGN (CD209), a C-type lectin receptor predominantly expressed on dendritic cells and select macrophage subsets, where it mediates calcium-dependent recognition of high-mannose and fucosylated glycans. Through ligand binding and internalization, DC-SIGN shapes antigen uptake, endosomal routing, and antigen presentation while coordinating innate–adaptive immune crosstalk. Signaling and trafficking downstream of DC-SIGN intersect with pathways controlling dendritic cell maturation, cytokine production, and pathogen sensing, influencing the quality of T cell priming. Altered DC-SIGN activity and expression have been implicated in immune evasion by glycosylated microbes and in inflammatory contexts where dendritic cell activation states contribute to disease-associated immune dysregulation.

DC-SIGN CRISPR Activation Plasmid (h) provides a targeted, non-destructive approach to upregulating endogenous CD209 expression without altering the underlying DNA sequence.

DC-SIGN CRISPR Activation Plasmid (h) is a three-plasmid synergistic activation mediator (SAM) system engineered for highly efficient, site-specific transcriptional upregulation of the CD209 locus in human cell lines. The system is built around a catalytically inactive Cas9 (dCas9) carrying two inactivating mutations (D10A and N863A) that eliminate nuclease activity while preserving DNA binding. This dCas9 is fused to VP64, a potent transcriptional activator, and is co-expressed with a blasticidin resistance gene for selection. The second plasmid encodes the MS2-p65-HSF1 fusion protein, a secondary activator complex that works in concert with dCas9-VP64, alongside a hygromycin resistance gene. The third plasmid encodes a target-specific 20 nt sgRNA fused to two MS2 RNA aptamers that recruit the MS2-p65-HSF1 complex to the activation site, accompanied by a puromycin resistance gene. The three plasmids are delivered at a 1:1:1 mass ratio for balanced expression of all system components.

Once assembled at the target locus, the SAM complex binds within approximately 200 bp upstream of the CD209 transcriptional start site, where VP64, p65, and HSF1 act in concert to recruit transcriptional machinery and drive upregulation of endogenous DC-SIGN expression. Unlike nuclease-active Cas9, dCas9 does not introduce double-strand breaks or modify the genomic sequence, preserving the native CD209 locus and enabling the study of DC-SIGN-dependent transcriptional responses at the endogenous locus, making it a valuable tool for functional studies, target gene identification, and the modeling of DC-SIGN pathway restoration in tumor cells with silenced or reduced CD209 expression.

For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.