PDIA3, also known as protein disulfide-isomerase A3, is a protein of the endoplasmic reticulum that interacts with lectin chaperones calreticulin and calnexin to modulate folding of newly synthesized glycoproteins. This protein has protein disulfide isomerase activity. PDIA3 is also part of the major histocompatibility complex (MHC) class I peptide-loading complex (TAP1), which is essential for formation of the final antigen conformation and export from the endoplasmic reticulum to the cell surface. Recombinant human PDIA3 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.