ERP57 can interact with glycoproteins such as calnexin and calreticulin, playing an important role as a molecular chaperone during glycoprotein biosynthesis and folding [22], and also can promote the formation of intra- or intermolecular disulfide bonds during glycoprotein folding [58-60] to cope with excessive protein folding load and re-establish cellular homeostasis, and it has reported that ERP57 has shown clinical applications to endoplasmic reticulum stress associated diseases and cancer [61], disruption of ERP57 in mouse is lethal. This evidence concerns the gene CANX and cancer.