ERO1-Like Protein a/ERO1L Protein(C-6His) (recombinant human)

Protein Construction: Recombinant Human ERO1-Like Protein alpha is produced by our Mammalian expression system and the target gene encoding Glu24-His468 is expressed with a 6His tag at the C-terminus. Sequence: Glu24-His468. Fusion tag: C-6His Endotoxin: < 1.0 EU per µg as determined by the LAL method. Apparent Molecular Mass: 71 kDa. Protein function: ERO1-Like Protein a (ERO1L) is an enzyme that belongs to the EROs family. ERO1L is expressed at high level in esophagus and upper digestive tract. ERO1L is an essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. ERO1L acts by oxidizing directly P4HB/PDI isomerase through a direct disulfide exchange. It associates with ERP44, 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. ERO1L may be responsible for a significant proportion of reactive oxygen species (ROS) in the cell. ERO1L responses to temperature stimulus, protein thiol-disulfide exchange, protein folding with or without chaperone cofactor and transport. Protein function: Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. Required for the proper folding of immunoglobulins. Involved in 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. Plays an important role in ER stress-induced, CHOP-dependent apoptosis by activating the inositol 1,4,5-trisphosphate receptor IP3R1. [The UniProt Consortium]