Key Features:
High Sensitivity: Produces a strong signal-to-background ratio with >20-fold induction, ensuring accurate and reproducible readouts in CREB pathway studies.
Versatile Applications: Mimics endogenous Amylin3 signaling cascades through co-expression of CTR, RAMPs, and a CREB-responsive luciferase reporter. Suitable for screening applications, dose-response assays, and characterization of Amylin3-targeting compounds.
Stable Integration: Generated via co-transfection of CTR, RAMPs, and CREB-luciferase constructs alongside a hygromycin resistance vector. Antibiotic-resistant clones were screened with Cagrilintide, and the highest-responding clone was expanded for production.
 
The Amylin3/CREB Luciferase Reporter Stable Cell Line is a robust, assay-ready model designed to study Amylin3 receptor signaling with high sensitivity and reproducibility. Amylin3 is a heterodimeric receptor formed by CTR and RAMPs and belongs to the class B GPCR family. It is implicated in mediating downstream signaling of both amyloid-β (Aβ) and human amylin (hAmylin). Activation of Amylin3 stimulates intracellular cAMP production through Gs protein–mediated adenylate cyclase activity, ultimately driving CREB-dependent transcription.
Signosis developed this cell line by co-transfecting HEK293 cells with pCMV-based expression vectors encoding the calcitonin receptor (CTR), receptor activity-modifying proteins (RAMPs), and a CREB-driven firefly luciferase reporter, along with a hygromycin resistance vector. Following hygromycin selection, antibiotic-resistant clones were carefully screened for Cagrilintide-induced luciferase activity, and the clone showing the highest fold induction was selected and expanded for production.
This stable cell line expresses CTR, RAMPs, and a CREB-responsive luciferase reporter in a single, optimized system, providing researchers with a consistent and validated tool for Amylin3 signaling studies.
This stable cell line provides an ideal model for investigating the signaling pathways triggered by Aβ and hAmylin, and for exploring whether their cytotoxic effects are specifically mediated through the Amylin3 isoform of the amylin receptor, serves as a powerful in vitro tool for both basic research and translational applications in endocrinology, pharmacology, and metabolic disease research.