Thioredoxin from Escherichia coli is widely used in biochemical research due to its role in redox regulation and protein disulfide bond reduction. It is commonly employed as a reducing agent in enzymatic assays, particularly for maintaining the reduced state of proteins and enzymes in vitro. This protein is also utilized in the study of oxidative stress responses and cellular redox signaling pathways. Additionally, it serves as a crucial component in protein refolding experiments, helping to correct misfolded proteins by facilitating disulfide bond rearrangement. Its applications extend to molecular biology techniques, such as enhancing the activity of certain DNA polymerases in PCR, improving efficiency and accuracy.