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Human Polyclonal ERO1L Primary Antibody for ICC, IF - ABIN250958
Jeschke, Gauglitz, Song, Kulp, Finnerty, Cox, Barral, Herndon, Boehning: Calcium and ER stress mediate hepatic apoptosis after burn injury. in Journal of cellular and molecular medicine 2010
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Human Polyclonal ERO1L Primary Antibody for ELISA, WB - ABIN565457
Qiang, Wang, Farmer: Adiponectin secretion is regulated by SIRT1 and the endoplasmic reticulum oxidoreductase Ero1-L alpha. in Molecular and cellular biology 2007
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Human Monoclonal ERO1L Primary Antibody for IHC (p), ELISA - ABIN565458
Araki, Iemura, Kamiya, Ron, Kato, Natsume, Nagata: Ero1-? and PDIs constitute a hierarchical electron transfer network of endoplasmic reticulum oxidoreductases. in The Journal of cell biology 2013
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Mutation of Val101 of Ero1 alpha results in a reduced Endoplasmic reticulum , retarded oxidative protein folding and decreased H2O2 levels in the Endoplasmic reticulum of cervical cancer cells and further impairs cell migration, invasion, and tumor growth.
this study involving a gene-modification approach indicate that ERO1alpha is a major proliferation-enhancing factor in cancer cells and could be used as both a diagnostic biomarker of cancer exacerbation and a therapeutic target.
The authors show that endoplasmic reticulum oxidoreductin 1alpha (Ero1alpha), the pivotal sulfhydryl oxidase that catalyzes disulfide formation in the endoplasmic reticulum, is phosphorylated by Fam20C in the Golgi apparatus and retrograde-transported to the endoplasmic reticulum mediated by ERp44.
Authors investigated the influence of ERO1-alpha on expression of PD-L1 and immune escape and demonstrated that ERO1-alpha augmented the expression of PD-L1 via facilitation of oxidative protein folding within PD-L1. Authors showed that overexpression of ERO1-alpha increased HIF-1alpha protein expression, resulting in an increase of PD-L1 mRNA as well as protein.
High expression of ERO1L is associated with poor prognosis of patients with gastric cancer. These results indicate that ERO1L expression may be a clinically promising therapeutic target for prevention of gastric cancer.
ERO1alpha plays a crucial role in HSC proliferation via posttranslational modification of collagen and MT1-MMP
Study shows that ERO1L and NARS expression level are up-regulated in primary lung adenocarcinoma and identifies them with a potential to promote tumor metastasis and growth of cancer cells.
a mechanism of dual Ero1alpha regulation by dynamic redox interactions between PDI and the two Ero1alpha flexible loops that harbor the regulatory cysteines.
Expression of ERO1-alpha in MDA-MB-231 cells promotes tumour growth via promoting angiogenesis. Knockdown of ERO1-alpha inhibits secretion of VEGF by inhibition of oxidative protein folding. In triple-negative breast cancer cases, the expression of ERO1-alpha was upregulated and related to the number of the blood vessels. ERO1-alpha was a poor prognosis factor in triple-negative breast cancer.
FBXO6 as a functional E3 ubiquitin ligase for Ero1L that plays a critical role in inhibiting endoplasmic reticulum stress-induced apoptosis.
Data indicate a new mechanism of Ero1alpha regulation in which thiol-disulfide exchange at Cys208-Cys241 affects the stability of the Cys94-Cys131 inhibitory disulfide through allosteric and/or inter-molecular communication.
the cancer-associated ERO1-alpha regulates the expression of the MHC class I molecule via oxidative folding
Data suggest that expression of ERO1alpha (oxidoreductin-1-L-alpha) and CHOP (c/EBP-homologous protein) is up-regulated in liver of patients with acute liver failure.
These results suggest that overexpression of ERO1-alpha in the tumor inhibits the T cell response by recruiting polymorphonuclear myeloid-derived suppressor cells
PDI has a role as a competent regulator and a specific substrate of Ero1alpha govern efficient and faithful oxidative protein folding and maintain the ER redox homeostasis
These results indicate that BPA, a widely distributed and potentially harmful chemical, inhibits Ero1-PDI-mediated disulfide bond formation.
The high expression of Ero1alpha in cancers of the esophagus and stomach demonstrates the importance of ER redox regulation in the gastro-intestinal (GI) tract in health and disease.
GPx7 promotes oxidative protein folding, directly utilizing Ero1alpha-generated hydrogen peroxide in the early secretory compartment.
A simple feedback mechanism of regulation of Ero1alpha was identified involving its primary substrate.
The expression of hERO1-alpha in cancer cells is associated with poorer prognosis.
this study shows that the hypoxia-inducible ER-resident oxidase ERO1-alpha plays an important role in the hypoxia-induced augmentation of MHC class I-peptide complex expression
Data (including data from knockout mice) suggest that up-regulation of expression of ERO1alpha (oxidoreductin-1-L-alpha) and CHOP (c/EBP-homologous protein) is involved in liver apoptosis/necrosis exhibited in acute liver failure.
ER stress induced by misfolded proinsulin was limited by increased expression of Ero1alpha, suggesting that enhancing the oxidative folding of proinsulin may be a viable therapeutic strategy in the treatment of type 2 diabetes.
combined loss-of-function mutations in genes encoding the ER thiol oxidases ERO1alpha, ERO1beta, and PRDX4 compromised the extracellular matrix and interfered with the intracellular maturation of procollagen
The peak amplitude of calcium transients in homozygous Ero1alpha mutant adult cardiomyocytes was reduced to 42.0 +/- 2.2% (n=10, P = 0.01) of values recorded in wild-type cardiomyocytes.
Describes mouse Ero1-l in addition to the human gene.
Oxygen regulation of ERO1-Lalpha expression likely maintains the transfer rate of oxidizing equivalents to PDI in situations of an altered cellular redox state induced by changes in the cellular oxygen tension
Endoplasmic reticulum oxidation 1 (ERO1) is a conserved eukaryotic flavin adenine nucleotide-containing enzyme that promotes disulfide bond formation.
Data suggest that ERp44 and Ero1-lalpha play a major role in the assembly of higher-order adiponectin complexes, and highlight the importance of posttranslational events controlling adiponectin levels and the release of adiponectin from adipocytes.
The endoplasmic reticulum (ER) oxidoreductase Ero1-L alpha and effectors modulating peroxisome proliferator-activated receptor gamma (PPAR gamma) and SIRT1 activities regulate secretion of adiponectin from 3T3-L1 adipocytes.
These data shed new light on how the CHOP pathway of apoptosis triggers calcium-dependent apoptosis through an ERO1-alpha-IP3R pathway.
Tissue distribution analysis of Ero1L and ERp44 genes revealed extremely high expression in adipose tissue, and the topology of their phylogenic tree indicates a high degree of conservation among different species.
This gene encodes a member of the endoplasmic reticulum oxidoreductin family. The encoded protein is localized to the endoplasmic reticulum and promotes the formation of disulfide bonds by oxidizing protein disulfide isomerase. This gene may play a role in endoplasmic reticulum stress-induced apoptosis and the cellular response to hypoxia.
, ERO1-like beta
, ERO1-like protein alpha
, Endoplasmic oxidoreductin-1-like protein
, ERO1-like (S. cerevisiae)
, endoplasmic oxidoreductin-1-like protein
, endoplasmic reticulum oxidation 1
, endoplasmic reticulum oxidoreductin-1-like protein
, global ischemia-induced protein 11