TCP1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 576 amino acids (1-556 a.a.) and having a molecular mass of 62.5kDa. The TCP1 is purified by proprietary chromatographic techniques.
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 complex consists of 2 identical stacked rings, each containing eight different proteins. Unfolded polypeptides penetrate the central cavity of the complex and are folded in an ATP-dependent manner. The TCP1 protein is found in the cytosol as a subunit of a hetero-oligomeric chaperone. TCP1 has a significant function in maintaining cellular homoeostasis by assisting the folding of many proteins such as the cytoskeletal components actin and tubulin.