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ER Stress and UPR

ER Stress and UPR

Focus Biomolecules offers a comprehensive offering of small molecule tools for studying ER stress and UPR. Look to Focus for high quality and affordable reagents for your important research. Feel free to contact us to discuss your needs today.

The endoplasmic reticulum (ER) is tasked with the productive folding of secretory and transmembrane proteins along with the regulation of ER homeostasis. These processes involve several highly coordinated activities which include chaperoning , folding, quality control and degradation mechanisms among others.1 Nascent proteins enter the ER where they undergo a process which, if successful results in correct folding and exiting the ER followed by migration to their final destination via the secretory pathway.2 However if folding fails, misfolded proteins are retained in the ER.3 When the misfolded protein burden becomes overwhelming, the condition results in ER stress. The cell has evolved to adapt to ER stress by engaging the unfolded protein response (UPR) pathway whose function is to restore protein homeostasis in the ER. If it fails the UPR will trigger signals to kill the cell via apoptosis.4 UPR can have a profound effect on normal and pathophysiology. Thus agents which target UPR may lead to new therapeutics.5

1.     Michalak (2002), Ca2+ Signaling and Calcium Binding Chaperones of the Endoplasmic Reticulum, Cell Calcium, 32 269
2.     Zhang (2004), Signaling the Unfolded Protein Response from the Endoplasmic Reticulum, J. Biol. Chem.,279 25935
3.     Ellgaard (2003), Quality Control in the Endoplasmic Reticulum, Nat Rev. Mol. Cell Biol., 4 181
4.     Hitomi (2004), Involvement of Caspase-4 in Endoplasmic Reticulum Stress-Induced Apoptosis and Abeta-Induced Cell Death, J. Cell Biol. 165 34
5.     Doultsinos (2017), Control of the Unfolded Protein Response in Health and Disease, SLAS Discovery 22 787


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