ER Stress/Unfolded Protein Response (UPR) Reagent Kit

The components of Cayman's ER Stress/UPR Reagent Kit enable the induction and selective modulation of ER stress and the UPR in cultured cells. Each reagent is supplied individually, allowing users to strategically combine inducers and modulators, as described below, to interrogate specific UPR branches (PERK, IRE1, and/or ATF6)., , Thapsigargin inhibits sarcoplasmic/endoplasmic reticulum Ca2+-ATPase (SERCA), causing depletion of calcium ions in the ER and impairment in chaperone function. This induces ER stress and robust UPR activation across PERK, IRE1, and ATF6 pathways., , Tunicamycin blocks N-linked glycosylation in the ER by inhibiting N-acetylglucosamine-1-phosphotransferase, leading to the accumulation of misfolded proteins and UPR activation through the PERK, IRE1, and ATF6 pathways.2, , Tauroursodeoxycholic acid (TUDCA) acts as a chemical chaperone that stabilizes protein folding in the ER, thereby reducing ER stress. It has commonly been used as a protective agent to broadly suppress UPR activation and prevent ER stress-mediated cell death.5, , Salubrinal inhibits the growth arrest and DNA damage-inducible protein 34-protein phosphatase 1 (GADD34-PP1) complex, preventing dephosphorylation of the PERK target eukaryotic translation initiation factor 2alpha (eIF2alpha). Phosphorylation of eIF2alpha by PERK leads to prolonged attenuation of protein translation and helps reduce ER protein-folding stress. Salubrinal can be used to evaluate the contribution of PERK signaling to the ER stress response., , KIRA6 is a selective inhibitor of IRE1alpha kinase activity that indirectly suppresses its RNase function. By blocking IRE1alpha signaling, KIRA6 reduces the IRE1-mediated UPR. KIRA6 can be used to evaluate the contribution of IRE1 signaling in ER stress., , Ceapin-A7 blocks the trafficking of ATF6 from the ER to the Golgi and thus inhibits its activation. Ceapin-A7 can be used to evaluate the role of ATF6 in ER stress.