This research article presents a simplified and cost-effective method for the expression and purification of recombinant human thyroid peroxidase (hTPO) from AD293 mammalian cells. The study focuses on improving protein yield and purity through a streamlined chromatographic purification approach, enabling the production of biologically active hTPO suitable for downstream diagnostic applications.

The purified hTPO was successfully validated using immunoblotting, enzymatic activity assay, ELISA, and competitive inhibition studies, confirming its structural integrity and functional activity. This work highlights the potential of recombinant hTPO as a reliable and economical diagnostic reagent for thyroid-related immunoassay development.