This recombinant protein corresponds to the mature form of mouse PDIA6 (also known as Thioredoxin domain-containing protein 7), encompassing amino acids 20–440 with the N-terminal signal peptide removed. It functions as a chaperone that inhibits aggregation of misfolded proteins and negatively regulates the unfolded protein response (UPR) by binding to UPR sensors such as ERN1 and EIF2AK3, thereby inactivating their signaling. PDIA6 also catalyzes the rearrangement of disulfide bonds in proteins and plays a role in platelet aggregation and activation in response to agonists like convulxin, collagen, and thrombin. This construct is designed for functional studies in vitro.