The Unfolded Protein Response (UPR) is a crucial stress response mechanism that cells use to deal with endoplasmic reticulum (ER) stress caused by the accumulation of misfolded proteins or faulty protein quality control. This stress response is conserved across different species and is activated to combat various diseases, including diabetes, Alzheimer's, Parkinson's, Huntingon's, and prion diseases.
 
During ER stress, the transcriptional upregulation of chaperone proteins is an early cellular response that is mediated by a large number of transcription factors (TFs). To facilitate the study of ER stress and UPR, Signosis has developed the Endoplasmic Reticulum Stress TF Activation Profiling Plate Array. This array can simultaneously monitor the activity of 16 ER stress/UPR related TFs, including XBP-1, ATF4, ATF6, GADD153/CHOP, CBF/NFY, SREBP1, YY1, ERR, ATF3, AP-1, FOXO1, IRF, p53, NFkB, NRF2/ARE, and HNF4.
 
By using this array, researchers can study the complex regulation of ER stress and UPR, identify potential therapeutic targets, and develop new treatments for diseases caused by ER stress. The Endoplasmic Reticulum Stress TF Activation Profiling Plate Array provides a valuable tool for investigating the molecular mechanisms underlying the UPR and its impact on cellular physiology and pathophysiology.
 
This image is extracted from our customer,  Laurentian University (https://zone.biblio.laurentian.ca/bitstream/10219/3774/1/MELISSA%20KAY%20-%20Final%20Thesis.pdf).