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ERO1L encodes a member of the endoplasmic reticulum oxidoreductin family. Additionally we are shipping ERO1-Like (S. Cerevisiae) Proteins (11) and many more products for this protein.
Showing 10 out of 93 products:
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 8 references for ABIN250958
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 references for ABIN565457
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
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.
GPx7 (show GPX7 Antibodies) promotes oxidative protein folding, directly utilizing Ero1alpha-generated hydrogen peroxide in the early secretory compartment.
Report on the establishment of an engineered CHOS cell line that has been engineered to express both XBP-1S) and ERO1-Lalpha and has been named CHOS-XE. CHOS-XE cells produced increased antibody (MAb) yields (5.3- 6.2 fold) in comparison to CHOS cells.
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.
Data indicate that protein disulfide isomerase (PDI (show P4HB Antibodies)) and ERp44 (show ERP44 Antibodies) dynamically localize Ero1alpha and peroxiredoxin 4 (show PRDX4 Antibodies) in early secretory compartment (ESC).
This paper reported the interactions of Ero1 with protein disulfide isomerase family proteins and chaperones, highlighting the effect that redox flux has on Ero1 partnerships.
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.
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 (show ERP44 Antibodies) and Ero1-lalpha play a major role in the assembly of higher-order adiponectin (show ADIPOQ Antibodies) complexes, and highlight the importance of posttranslational events controlling adiponectin (show ADIPOQ Antibodies) levels and the release of adiponectin (show ADIPOQ Antibodies) 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 (show ADIPOQ Antibodies) from 3T3-L1 adipocytes.
These data shed new light on how the CHOP (show DDIT3 Antibodies) pathway of apoptosis triggers calcium-dependent apoptosis through an ERO1-alpha-IP3R (show ITPR1 Antibodies) pathway.
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