Endoplasmic reticulum (ER) mediated cell stress and the unfolded protein response (UPR) serve as a major stress pathway in eukaryotic cells. ER stress and the UPR can be triggered by a number of cellular perturbations including misregulation of ER Ca2+, accumulation of misfolded proteins within the lumen of the ER, and reactive oxygen species. Activation of proteostatic pathways, such as the UPR and ER-stress serves as an early indicator of treatment-induced cell stress or toxicity. Combining automated live cell imaging and analysis with the reversible cell stress biosensor from Montana Molecular provides a sensitive and reversible method for detecting the UPR and ER-stress in real time.
- Thapsigargin-induced Cellular Stress Response and Inhibition of Gq-dependent Calcium Signaling
- Monitoring Cellular Stress Response and Inhibition of GPCR-Dependent Calcium Signaling Using Expressed Biosensors
- Live-Cell Assays for Cell Stress Responses Reveal New Patterns of Cell Signaling Caused by Mutations in Rhodopsin, α-Synuclein and TDP-43