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 various 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. This method is ideal for detecting the UPR and ER stress in real time.
Figure 1. Detection of UPR and ER stress over time.
- Thapsigargin-induced Cellular Stress Response and Inhibition of Gq-dependent Calcium Signaling
- Live-Cell Assays for Cell Stress Responses Reveal New Patterns of Cell Signaling Caused by Mutations in Rhodopsin, α-Synuclein and TDP-43
For Research Use Only. Not for use in diagnostic procedures.