Expression and Purification of Recombinant Human Amelogenin Using the Prokaryotic Expression System

Abstract

Abstract-The amelogenins (Am) constitute about 90% of the enamel matrix proteins and play a critical role in enamel biomineralization. This study aimed to express and characterize recombinant human amelogenin (rAm) protein in the prokaryotic expression system in quantities sufficient for structural and functional research. Human cDNA coding for a 175 amino acid amelogenin protein was subcloned into the pET-28a(+) vector, this system adds a hexa-histidine tag to N-terminal amino acid of the expressed protein, enabling effective three steps purification by Ni