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Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Additionally we are shipping ERO1-Like beta (S. Cerevisiae) Proteins (4) and many more products for this protein.
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glutathione limits Ero1-dependent oxidation in the endoplasmic reticulum
Ero1alpha and Ero1beta are retained in the endoplasmic reticulum by interactions with PDI (show PADI1 Antibodies) and ERp44 (show ERP44 Antibodies)
the Ero (show OPN3 Antibodies) FAD (show BRCA2 Antibodies) binding domain is critical for conformational stability, allowing Ero (show OPN3 Antibodies) proteins to withstand stress conditions that cause client proteins to misfold
The lack of correlation between changes in SAT adiponectin (show ADIPOQ Antibodies) gene and protein expression and its circulating levels suggests that adipose tissue synthesis and release of adiponectin (show ADIPOQ Antibodies) are highly regulated pathways.
combined loss-of-function mutations in genes encoding the ER thiol oxidases ERO1alpha, ERO1beta, and PRDX4 (show PRDX4 Antibodies) compromised the extracellular matrix and interfered with the intracellular maturation of procollagen
Several lines of evidence suggest that ERO1lbeta is involved in maintaining insulin (show INS Antibodies) content of pancreatic beta cells and in regulating beta cell survival during ER oxidative stress.
An unexpectedly selective function for ERO1-beta in oxidative protein folding in insulin (show INS Antibodies)-producing cells that is required for glucose homeostasis in vivo.
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 being a source of oxidative stress. Required for the folding of cell, thereby being a source of oxidative stress.
ERO1-like protein beta
, ERO1-like beta (S. cerevisiae)
, endoplasmic reticulum oxidoreductin 1-Lbeta
, ERO1-like protein beta-like
, endoplasmic oxidoreductin-1-like protein B
, endoplasmic oxidoreductase 1 beta