Proteins expressed in the endoplasmic reticulum (ER) are tightly regulated by a variety of quality control mechanisms. Terminally misfolded proteins in the ER are retrotranslocated to the cytoplasm and degraded by proteasomes through a mechanism known as ER-associated degradation (ERAD). EDEM2 (ER degradation-enhancing alpha-mannosidase-like 2) is a 578 amino acid secreted protein that, in conjunction with other EDEM proteins (namely EDEM and EDEM3), is involved in the ERAD pathway of protein degradation. EDEM2, a member of the glycosyl hydrolase 47 family, contains a mannosidase homology domain, an N-terminal cleavable signal sequence and a C-terminal extension that is required for both ER retention and the proper function of EDEM2. Human EDEM2 shares 93% sequence identity with its mouse homolog, suggesting a conserved role between species. Two isoforms of EDEM2 exist due to alternative splicing events.