ERp72 (human), (recombinant) (His-tag)

Endoplasmic reticulum protein (ERp) 72 is a member of the protein disulfide isomerase (PDI) family that is localized to the endoplasmic reticulum. It contains three repeats of the thioredoxin-like regions that is postulated to represent three independently acting catalytic domains (CGHC) of PDI activity. ERp72 contains the sequence at its carboxyl terminus which serves as its ER retention signal. Together with other ER resident proteins such as BiP, GRP94, and PDI, they serve as the molecular chaperones for proper folding of newly translocated and glycolsylated proteins such as thyroglobulin (Tg) and human chorionic gonadotropin (hCG)-b. ERp72 expression is regulated by the level of misfolding proteins in the ER, as the amount of ERp72 increased in response to epithelial ischemia, a condition that perturbs the maturation of secretory proteins.