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ERO1L, also named as ERO1-alpha, is an essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. It acts by oxidizing directly P4HB/PDI isomerase through a direct disulfide exchange. It does not act as a direct oxidant of folding substrate, but relies on P4HB/PDI to transfer oxidizing equivalent. Associates with ERP44 but not with GRP54, demonstrating that it does not oxidize all PDI related proteins and can discriminate between PDI and related proteins. Its reoxidation probably involves electron transfer to molecular oxygen via FAD. Glutathione may be required to regulate its activity in the endoplasmic reticulum. It may be responsible for a significant proportion of reactive oxygen species (ROS) in the cell, thereby being a source of oxidative stress. It is required for the folding of immunoglobulin proteins. Responsible for the release of the unfolded cholera toxin from reduced P4HB/PDI in case of infection by V.cholerae, thereby playing a role in retrotranslocation of the toxin. This antibody has no cross reaction to ERO1L.