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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
Show all 9 Pubmed References
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
Show all 2 Pubmed References
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
Show all 2 Pubmed References
ERO1alpha plays a crucial role in HSC (show FUT1 Antibodies) proliferation via posttranslational modification of collagen and MT1-MMP (show MMP14 Antibodies)
Study shows that ERO1L and NARS (show NARS Antibodies) 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 (show PADI1 Antibodies) 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 (show VEGFA Antibodies) 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 (show FBXO6 Antibodies) as a functional E3 ubiquitin ligase (show MUL1 Antibodies) for Ero1L that plays a critical role in inhibiting endoplasmic reticulum stress-induced apoptosis.
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 liv (show DDIT3 Antibodies)er 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 (show PADI1 Antibodies) 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 (show DST Antibodies), a widely distributed and potentially harmful chemical, inhibits Ero1-PDI (show PADI1 Antibodies)-mediated disulfide bond formation.
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 (show DDIT3 Antibodies)) is involved in liver apoptosis/necrosis exhibited in acute liver failure.
ER stress induced by misfolded proinsulin (show INS Antibodies) was limited by increased expression of Ero1alpha, suggesting that enhancing the oxidative folding of proinsulin (show INS Antibodies) 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 (show PRDX4 Antibodies) compromised the extracellular matrix and interfered with the intracellular maturation of procollagen
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 (show PDIA3 Antibodies) 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 (show HSD17B6 Antibodies) Ero1-L alpha and effectors modulating peroxisome proliferator-activated receptor gamma (PPAR gamma (show PPARG Antibodies)) and SIRT1 (show SIRT1 Antibodies) activities regulate secretion of adiponectin from 3T3-L1 adipocytes.
Tissue distribution analysis of Ero1L and ERp44 (show ERP44 Antibodies) 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