PURIFICATION OF A RECOMBINANT GFP-PREPTIN FUSION PROTEIN**

Authors

Apoorva Kollaram*, Columbus State University, Columbus, GA 31907Follow
Chayce C. Schuler*Follow
Jonathan M. MeyersFollow

Abstract

The osteogenic hormone preptin is an attractive target for the treatment of both osteoporosis and Type II diabetes. Typically this 34 amino acid peptide is produced via solid-phase peptide synthesis, which requires expensive solvents and instruments. We report the cloning and recombinant production of a GFP-Preptin (rat) fusion protein in E. coli(BL21). The fusion protein was isolated for biochemical characterization using low-pressure nickel affinity chromatography.

Recommended Citation

Kollaram*, Apoorva; Schuler*, Chayce C.; and Meyers, Jonathan M. (2024) "PURIFICATION OF A RECOMBINANT GFP-PREPTIN FUSION PROTEIN**," Georgia Journal of Science, Vol. 82, No. 1, Article 47.
Available at: https://digitalcommons.gaacademy.org/gjs/vol82/iss1/47