CysLT₁ Receptor CRISPR Activation Plasmid (h): sc-416516-ACT

CYSLTR1 encodes the human cysteinyl leukotriene receptor 1 (CysLT1 receptor), a G protein–coupled receptor that binds LTC4, LTD4, and LTE4 to transduce inflammatory lipid mediator signals. Upon activation it primarily couples to Gq/11 to stimulate phospholipase C signaling, intracellular Ca2+ mobilization, and downstream MAPK and NF-κB–linked transcriptional programs that regulate chemotaxis, vascular permeability, and smooth muscle contractility. CYSLTR1 activity intersects with arachidonic acid/leukotriene biosynthesis pathways and shapes leukocyte–stromal communication within inflamed tissues. Dysregulated CysLT1 receptor signaling has been associated with airway inflammation and remodeling, allergic responses, and broader immune-mediated pathologies, supporting its use as a mechanistic node in inflammation research.

CysLT1 Receptor CRISPR Activation Plasmid (h) provides a targeted, non-destructive approach to upregulating endogenous CYSLTR1 expression without altering the underlying DNA sequence.

CysLT1 Receptor CRISPR Activation Plasmid (h) is a three-plasmid synergistic activation mediator (SAM) system engineered for highly efficient, site-specific transcriptional upregulation of the CYSLTR1 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 CYSLTR1 transcriptional start site, where VP64, p65, and HSF1 act in concert to recruit transcriptional machinery and drive upregulation of endogenous CysLT1 Receptor expression. Unlike nuclease-active Cas9, dCas9 does not introduce double-strand breaks or modify the genomic sequence, preserving the native CYSLTR1 locus and enabling the study of CysLT1 Receptor-dependent transcriptional responses at the endogenous locus, making it a valuable tool for functional studies, target gene identification, and the modeling of CysLT1 Receptor pathway restoration in tumor cells with silenced or reduced CYSLTR1 expression.

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