cadherin-26 CRISPR Activation Plasmid (h2): sc-401989-ACT-2

Human CDH26 encodes cadherin-26, a calcium-dependent cell–cell adhesion protein that contributes to epithelial barrier organization and intercellular junctional stability through homophilic cadherin interactions. CDH26 activity intersects with adhesion-linked signaling networks, including cytoskeletal remodeling and junction-associated pathways that shape tissue architecture and immune–epithelial crosstalk. Altered CDH26 expression has been reported in inflammatory and allergic contexts, supporting investigation of its role in mucosal biology, airway and gastrointestinal epithelium function, and barrier-associated remodeling. CDH26 gene editing or perturbation enables mechanistic studies of epithelial differentiation, adhesion dynamics, and downstream transcriptional programs using relevant in vitro and in vivo human model systems.

cadherin-26 CRISPR Activation Plasmid (h2) provides a targeted, non-destructive approach to upregulating endogenous CDH26 expression without altering the underlying DNA sequence.

cadherin-26 CRISPR Activation Plasmid (h2) is a three-plasmid synergistic activation mediator (SAM) system engineered for highly efficient, site-specific transcriptional upregulation of the CDH26 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 CDH26 transcriptional start site, where VP64, p65, and HSF1 act in concert to recruit transcriptional machinery and drive upregulation of endogenous cadherin-26 expression. Unlike nuclease-active Cas9, dCas9 does not introduce double-strand breaks or modify the genomic sequence, preserving the native CDH26 locus and enabling the study of cadherin-26-dependent transcriptional responses at the endogenous locus, making it a valuable tool for functional studies, target gene identification, and the modeling of cadherin-26 pathway restoration in tumor cells with silenced or reduced CDH26 expression.

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