Scientists engineered E. coli bacteria to produce human thymosin alpha-1 as a fusion protein, achieving yields of about 35-40% of total cellular protein. After simple chemical cleavage, approximately 0.2 grams per liter of thymosin alpha-1 could be harvested, and testing confirmed the recombinant product had full biological activity matching the native peptide. This efficient production method could help make thymosin alpha-1 more widely available for therapeutic use.
Xiu, Zhao-Yang; Yu, Ying; Chen, Chang-Qing