Transferrin acts as a vehicle for iron transportation between the absorption, storage and utilization sites in the body and, besides iron, its two highaffinity iron-binding site are capable of binding to 29 other elements. In physiological and pathophysiological conditions, transferrin’s properties are different and close attention to these properties is required. For further investigation for the above properties, it is necessary to have this protein in highly pure state.The purpose of this research was to isolate and purify the human transferrin from serum with native properties and high purity. The results of this research lead to a protocol for the isolation and purification of human transferrin which is cost-effective and time saving to produce antitransferrin antibody for immunological kits.