SSTR2 CRISPR Activation Plasmid (h): sc-401618-ACT

Somatostatin receptor 2 (SSTR2) is a Gi/o-coupled G protein–coupled receptor that mediates the inhibitory actions of somatostatin on hormone secretion, neuronal excitability, and cell signaling. Upon ligand engagement, SSTR2 suppresses adenylyl cyclase to reduce cAMP/PKA signaling, modulates ion channel activity, and can engage MAPK/ERK and PI3K-associated pathways with context-dependent effects on proliferation and differentiation. Receptor internalization and recycling/desensitization via β-arrestin–linked processes further shape signaling dynamics and cellular responsiveness. Altered SSTR2 expression is widely used as a molecular feature in neuroendocrine biology and tumor model systems, supporting studies of receptor trafficking, endocrine regulation, and GPCR network rewiring.

SSTR2 CRISPR Activation Plasmid (h) provides a targeted, non-destructive approach to upregulating endogenous SSTR2 expression without altering the underlying DNA sequence.

SSTR2 CRISPR Activation Plasmid (h) is a three-plasmid synergistic activation mediator (SAM) system engineered for highly efficient, site-specific transcriptional upregulation of the SSTR2 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 SSTR2 transcriptional start site, where VP64, p65, and HSF1 act in concert to recruit transcriptional machinery and drive upregulation of endogenous SSTR2 expression. Unlike nuclease-active Cas9, dCas9 does not introduce double-strand breaks or modify the genomic sequence, preserving the native SSTR2 locus and enabling the study of SSTR2-dependent transcriptional responses at the endogenous locus, making it a valuable tool for functional studies, target gene identification, and the modeling of SSTR2 pathway restoration in tumor cells with silenced or reduced SSTR2 expression.

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