ERO1L Products

Description

Perhaps the most distinctive feature of protein folding in the ER is the abundance of disulfide bonds that must form during maturation of proteins traveling along the secretory pathway. Formation of disulfide bonds is a redox reaction. Thus, to match the flux of disulfide bonds that exit from the ER by virtue of protein secretion, a flux of oxidizing equivalents into the ER is required. In eukaryotic cells, the essential protein relay supporting this flux, and hence disulfide bond formation, involves endoplasmic reticulum oxidoreductin 1 (Ero1) and protein disulfide isomerase (PDI). The temporal pattern of hypoxic ERO1-L alpha induction is very similar to that of genes triggered by the hypoxia inducible transcription factor (HIF-1) and is characteristically mimicked by cobalt and by deferoxamine, but is absent in cells with a defective aryl hydrocarbon receptor translocator (ARNT, HIF-1 alpha). We speculate from these findings that the expression of ERO1-L alpha is probably regulated via the HIF-pathway and thus belongs to the family of classic oxygen regulated genes.

Bioinformatics

Entrez	171562 Rat 30001 Human 50527 Mouse
Uniprot	AAH08674.1 Human NP_055399 Human Q96HE7 Human
Product By Gene ID	30001
Alternate Names	EC 1.8.4 EC 1.8.4.- Endoplasmic oxidoreductin-1-like protein ERO1 (S. cerevisiae)-like ERO1A ERO1-alpha ERO1-L ERO1-L-alpha ERO1-like (S. cerevisiae) ERO1-like protein alpha Oxidoreductin-1-L-alpha oxidoreductin-1-L-alpha

Research Areas for ERO1L

Find related products by research area and learn more about each of the different research areas below.

Cancer
ER Markers
Hypoxia
Membrane Trafficking and Chaperones
Signal Transduction

Related ERO1L Blog Posts

Check out the latest blog posts on ERO1L.

ERO1 Activity: A Potential Source of ER-Derived Oxidative Stress. Disulfide bond formation is a pivotal step in the maturation and release of secretory proteins that are controlled by specific endoplasmic reticulum (ER) resident enzymes. An important element in this process is ERO (ER oxidoreduction), a glycosylated...    Read more.

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