How do I detect ER stress?
Posted August 25, 2021
Excessive accumulation of misfolded proteins in the endoplasmic reticulum (ER) is the main cause of ER stress.
ER stress is detected using Thioflavin T (ThT). This is a relatively new method that is being used to detect endoplasmic reticulum (ER) stress in live cells.
Thioflavin T is a tiny molecule that exhibits enhanced fluorescence on binding to protein aggregates. The enhanced ThT-fluorescence correlates directly with proven indicators of UPR (unfolded protein response) activation. Thioflavin T enables researchers to detect ER stress induced by a variety of conditions and compounds within 20 minutes of applying the ER-stress inducing agent.
ER stress can also be detected indirectly by measuring the levels of specific UPR factors. Commonly measured indicators of UPR activation include: phosphorylated PERK, phosphorylated eIF2α, Gadd153/CHOP, ATF4, Grp78/BiP, Grp94, calreticulin, and protein disulphide isomerase (PDI). These are usually detected by immunoblot or immunohistochemistry.
Detection and quantification of endoplasmic reticulum stress in living cells using the fluorescent compound, Thioflavin T
Cell Navigator™ Live Cell Endoplasmic Reticulum (ER) Staining Kit *Red Fluorescence*