ERO1-Like Protein Alpha (ERO1L) ELISA Kit for Rat

ERO1L: Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly P4HB/PDI isomerase through a direct disulfide exchange. 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. Acts independently of glutathione. May be responsible for a significant proportion of reactive oxygen species (ROS) in the cell, thereby being a source of oxidative stress. 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. Predominantly monomer. May function both as a monomer and a homodimer. Interacts with PDILT. Stimulated by hypoxia; suggesting that it is regulated via the HIF-pathway. Widely expressed at low level. Expressed at high level in upper digestive tract. Highly expressed in esophagus. Weakly expressed in stomach and duodenum. Enzyme activity is tightly regulated to prevent the accumulation of reactive oxygen species in the endoplasmic reticulum. Reversibly down-regulated by the formation of disulfide bonds between the active site Cys-94 and Cys-131, and between Cys- 99 and Cys-104. Glutathione may be required to regulate its activity in the endoplasmic reticulum. Belongs to the EROs family.

Protein type: EC 1.8.4.-; Oxidoreductase; Secreted; Secreted, signal peptide

Chromosomal Location of Human Ortholog: 15p14

Cellular Component: dendrite; endoplasmic reticulum; endoplasmic reticulum membrane; intracellular; membrane

Molecular Function: oxidoreductase activity; oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; protein disulfide isomerase activity; protein disulfide oxidoreductase activity

Biological Process: 4-hydroxyproline metabolic process; brown fat cell differentiation; cell redox homeostasis; cellular protein modification process; chaperone cofactor-dependent protein folding; endoplasmic reticulum unfolded protein response; extracellular matrix organization; organ senescence; protein folding; protein maturation via protein folding; release of sequestered calcium ion into cytosol