Osteoporosis is a bone disease characterized by deficiencies in bone microstructure and decreased bone mass density. Teriparatide is a peptide derived from parathyroid hormone. Teriparatide was approved by the FDA in 2002 for the treatment of osteoporosis and following its patent expiration, companies are racing to produce teriparatide as biosimilar. The challenge of peptide production by recombinant methods is that the host's proteases easily degrade the peptide due to the peptide's small size and lack of defined structure. To overcome this problem, using a fusion tag is suggested for teriparatide production in the literature. This project aims to produce biosimilar teriparatide molecule with a novel construct: NTL9-teriparatide fusion protein. Production was done in E. coli with a plasmid designed: NTL9 (N-terminal domain of ribosomal protein L9, the fusion partner is a solubility-enhancing tag), TEV protease cleavage site, and teriparatide peptide. The fusion protein NTL9-teriparatide was purified after production and was verified with mass spectrometry. The most efficient production condition was 30°C in TB media with 1 mM of IPTG. We got 35 mg/L fusion protein. Regarding purification, Ni-NTA affinity chromatography was used first, followed by ion exchange chromatography. 98.3% of the fusion protein and 100% of teriparatide peptide was confirmed by LC-MS. Teriparatide was cleaved from the fusion protein using TEV protease under various conditions, including incubation times of 1 hour to 3 days at 4°C and 30°C, but cleavage efficiency remained a challenge. Optimization of TEV protease cleavage of the fusion protein will continue in Dr. Taşkent Sezgin's laboratory.