The lectin chaperones calnexin (CNX) and calreticulin (CRT) localized in the 
endoplasmic reticulum play important roles in glycoprotein quality control. 
Although the interaction between these lectin chaperones and ERp57 is well 
known, it has been recently reported that endoplasmic reticulum protein 29 
(ERp29), a member of PDI family, interacts with CNX and CRT. The biochemical 
function of ERp29 is unclear because it exhibits no ERp57-like redox activity. 
In this study, we addressed the possibility that ER chaperones CNX and CRT are 
connected via ERp29, based on our observation that ERp29 exists as a dimer. As a 
result, we showed that CNX dimerizes through ERp29. These results endorse the 
hypothesis that ERp29 serves as a bridge that links two molecules of CNX. Also, 
we showed that similar complexes such as CNX-CRT were formed via ERp29.