SSTR1 CRISPR Activation Plasmid (h): sc-403410-ACT

Somatostatin receptor 1 (SSTR1) is a Gi/o-coupled G protein–coupled receptor that binds somatostatin peptides to modulate adenylate cyclase activity and reduce intracellular cAMP, thereby shaping downstream PKA signaling and transcriptional responses. SSTR1 activation can also influence ion channel conductance and engage MAPK/ERK and PI3K-associated signaling nodes in a context-dependent manner, affecting cellular excitability, secretion, and proliferation programs. In human tissues, SSTR1 contributes to neuroendocrine signaling and regulatory feedback across endocrine and nervous system circuits. Dysregulated somatostatin receptor signaling has been studied in relation to altered hormone release and receptor-dependent growth control in models relevant to neuroendocrine and neurological disease biology.

SSTR1 CRISPR Activation Plasmid (h) provides a targeted, non-destructive approach to upregulating endogenous SSTR1 expression without altering the underlying DNA sequence.

SSTR1 CRISPR Activation Plasmid (h) is a three-plasmid synergistic activation mediator (SAM) system engineered for highly efficient, site-specific transcriptional upregulation of the SSTR1 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 SSTR1 transcriptional start site, where VP64, p65, and HSF1 act in concert to recruit transcriptional machinery and drive upregulation of endogenous SSTR1 expression. Unlike nuclease-active Cas9, dCas9 does not introduce double-strand breaks or modify the genomic sequence, preserving the native SSTR1 locus and enabling the study of SSTR1-dependent transcriptional responses at the endogenous locus, making it a valuable tool for functional studies, target gene identification, and the modeling of SSTR1 pathway restoration in tumor cells with silenced or reduced SSTR1 expression.

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