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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 and many more products for this protein.
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This peptide, Ac-VDTTD-AFC, was efficiently cleaved by purified caspase-2 and auto-activating caspase-2 in mammalian cells, and exhibited better selectivity for caspase-2 relative to caspase-3 than reagents that are currently available.
GJB2 and ERO1LB are implicated in pancreatic cancer progression and can be used to predict patient survival
upregulated in pancreatic neuroendocrine tumors
In the present work, it was shown that recombinant human Ero1beta is twice as active as Ero1alpha in enzymatic assays.
glutathione limits Ero1-dependent oxidation in the endoplasmic reticulum
analysis of Ero1beta tissue distribution and dimerization
Ero1alpha and Ero1beta are retained in the endoplasmic reticulum by interactions with PDI and ERp44
the Ero FAD binding domain is critical for conformational stability, allowing Ero proteins to withstand stress conditions that cause client proteins to misfold
The lack of correlation between changes in SAT adiponectin gene and protein expression and its circulating levels suggests that adipose tissue synthesis and release of adiponectin are highly regulated pathways.
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