LRIG2 CRISPR Activation Plasmid (h): sc-404443-ACT

LRIG2 (leucine-rich repeats and immunoglobulin-like domains 2) is a single-pass transmembrane protein implicated in modulation of receptor tyrosine kinase signaling at the cell surface, influencing downstream pathways that regulate proliferation, differentiation, and survival. Through its extracellular LRR/Ig-like domains, LRIG2 is positioned to shape the amplitude and duration of growth factor responses, with functional links reported for EGFR/ERBB family–associated signaling contexts. Altered LRIG2 expression has been observed in multiple disease-associated transcriptional profiles, supporting its use as a mechanistic node for studying dysregulated signaling, cell fate control, and microenvironmental interactions in human cells. These properties make LRIG2 a relevant target for interrogating membrane-proximal pathway regulation and gene expression programs associated with abnormal cellular growth.

LRIG2 CRISPR Activation Plasmid (h) provides a targeted, non-destructive approach to upregulating endogenous LRIG2 expression without altering the underlying DNA sequence.

LRIG2 CRISPR Activation Plasmid (h) is a three-plasmid synergistic activation mediator (SAM) system engineered for highly efficient, site-specific transcriptional upregulation of the LRIG2 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 LRIG2 transcriptional start site, where VP64, p65, and HSF1 act in concert to recruit transcriptional machinery and drive upregulation of endogenous LRIG2 expression. Unlike nuclease-active Cas9, dCas9 does not introduce double-strand breaks or modify the genomic sequence, preserving the native LRIG2 locus and enabling the study of LRIG2-dependent transcriptional responses at the endogenous locus, making it a valuable tool for functional studies, target gene identification, and the modeling of LRIG2 pathway restoration in tumor cells with silenced or reduced LRIG2 expression.

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