PDIA6 is a member of the protein disulfide isomerase (PDI). PDI is an enzyme in the endoplasmic reticulum in eukaryotes or periplasmic space of prokaryotes that catalyzes the formation and breakage of disulfide bonds between cysteine residues within proteins as they fold. PDIA6 function as a chaperone that inhibits aggregation of misfolded proteins. It plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin. Recombinant human PDIA6 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.