ATF-6 Recombinant Rabbit mAb (S-4366)

ATF-6 protein (activating transcription factor 6) is a key transmembrane protein in the endoplasmic reticulum (ER), belonging to the basic leucine zipper (bZIP) transcription factor family, and plays a central regulatory role in the ER unfolded protein response. Under normal conditions, ATF-6 remains inactive by binding to the molecular chaperone BiP. When the accumulation of misfolded or unfolded proteins in the ER triggers ER stress, BiP dissociates from ATF-6, allowing ATF-6 to translocate to the Golgi apparatus, where it is sequentially cleaved by site-1 protease and site-2 protease, releasing its cytosolic domain—the activated transcription factor form. This activated fragment then enters the nucleus, binds to ER stress response elements, and upregulates the expression of various genes, including those encoding molecular chaperones, foldases, and ER-associated degradation pathway components, thereby enhancing ER protein folding capacity, alleviating stress, and restoring cellular homeostasis. Furthermore, ATF-6 is involved in regulating cell differentiation, lipid metabolism, and antioxidant responses. Dysfunction of ATF-6 is closely associated with various diseases, including diabetes, neurodegenerative diseases (such as Alzheimer's and Parkinson's diseases), and certain cancers. Therefore, ATF-6 is not only a key regulator for maintaining ER functional integrity but also an important potential therapeutic target for these diseases.