TCP1 is a molecular chaperone that is a member of the chaperonin containing TCP1 complex (CCT), also known as the TCP1 ring complex (TRiC). This protein is found in the cytosol as a subunit of a hetero-oligomeric chaperone. It has an important function in maintaining cellular homoeostasis by assisting the folding of many proteins, including the cytoskeletal components actin and tubulin. Recombinant human TCP1 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography.