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ERO1-Like (S. Cerevisiae) Proteins (ERO1L)

ERO1L encodes a member of the endoplasmic reticulum oxidoreductin family. Additionally we are shipping ERO1-Like (S. Cerevisiae) Antibodies (90) and many more products for this protein.

list all proteins Gene Name GeneID UniProt
ERO1L 30001 Q96HE7
ERO1L 50527 Q8R180
ERO1L 171562 Q8R4A1
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Top ERO1-Like (S. Cerevisiae) Proteins at antibodies-online.com

Showing 9 out of 11 products:

Catalog No. Origin Source Conjugate Images Quantity Supplier Delivery Price Details
HOST_Escherichia coli (E. coli) Mouse His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Log in to see 29 to 34 Days
$4,331.68
Details
HOST_Escherichia coli (E. coli) Human His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Log in to see 29 to 34 Days
$4,331.68
Details
HOST_Wheat germ Human GST tag 10 μg Log in to see 9 Days
$405.71
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Yeast Rat His tag   1 mg Log in to see 56 to 66 Days
$3,234.00
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Yeast Xenopus tropicalis His tag   1 mg Log in to see 56 to 66 Days
$3,246.83
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Yeast Wild boar His tag   1 mg Log in to see 56 to 66 Days
$3,246.83
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Yeast Cow His tag   1 mg Log in to see 56 to 66 Days
$3,246.83
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Yeast Zebrafish His tag   1 mg Log in to see 56 to 66 Days
$3,322.00
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HOST_Human Human His tag   10 μg Log in to see 5 Days
$203.50
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ERO1L Proteins by Origin and Source

Origin Expressed in Conjugate
Human , ,
,
Mouse (Murine)

Rat (Rattus)

More Proteins for ERO1-Like (S. Cerevisiae) (ERO1L) Interaction Partners

Human ERO1-Like (S. Cerevisiae) (ERO1L) interaction partners

  1. the cancer-associated ERO1-alpha regulates the expression of the MHC class I molecule via oxidative folding

  2. 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 Proteins)er failure.

  3. These results suggest that overexpression of ERO1-alpha in the tumor inhibits the T cell response by recruiting polymorphonuclear myeloid-derived suppressor cells

  4. PDI (show PADI1 Proteins) 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

  5. These results indicate that BPA (show DST Proteins), a widely distributed and potentially harmful chemical, inhibits Ero1-PDI (show PADI1 Proteins)-mediated disulfide bond formation.

  6. GPx7 (show GPX7 Proteins) promotes oxidative protein folding, directly utilizing Ero1alpha-generated hydrogen peroxide in the early secretory compartment.

  7. 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.

  8. ER stress induced by misfolded proinsulin (show INS Proteins) was limited by increased expression of Ero1alpha, suggesting that enhancing the oxidative folding of proinsulin (show INS Proteins) may be a viable therapeutic strategy in the treatment of type 2 diabetes.

  9. Data indicate that protein disulfide isomerase (PDI (show P4HB Proteins)) and ERp44 (show ERP44 Proteins) dynamically localize Ero1alpha and peroxiredoxin 4 (show PRDX4 Proteins) in early secretory compartment (ESC).

  10. 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.

Mouse (Murine) ERO1-Like (S. Cerevisiae) (ERO1L) interaction partners

  1. 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 Proteins)) is involved in liver apoptosis/necrosis exhibited in acute liver failure.

  2. These results suggest that overexpression of ERO1-alpha in the tumor inhibits the T cell response by recruiting polymorphonuclear myeloid-derived suppressor cells

  3. ER stress induced by misfolded proinsulin (show INS Proteins) was limited by increased expression of Ero1alpha, suggesting that enhancing the oxidative folding of proinsulin (show INS Proteins) may be a viable therapeutic strategy in the treatment of type 2 diabetes.

  4. combined loss-of-function mutations in genes encoding the ER thiol oxidases ERO1alpha, ERO1beta, and PRDX4 (show PRDX4 Proteins) compromised the extracellular matrix and interfered with the intracellular maturation of procollagen

  5. Describes mouse Ero1-l in addition to the human gene.

  6. Oxygen regulation of ERO1-Lalpha expression likely maintains the transfer rate of oxidizing equivalents to PDI (show PDIA3 Proteins) in situations of an altered cellular redox state induced by changes in the cellular oxygen tension

  7. Endoplasmic reticulum oxidation 1 (ERO1) is a conserved eukaryotic flavin adenine nucleotide-containing enzyme that promotes disulfide bond formation.

  8. Data suggest that ERp44 (show ERP44 Proteins) and Ero1-lalpha play a major role in the assembly of higher-order adiponectin (show ADIPOQ Proteins) complexes, and highlight the importance of posttranslational events controlling adiponectin (show ADIPOQ Proteins) levels and the release of adiponectin (show ADIPOQ Proteins) from adipocytes.

  9. The endoplasmic reticulum (ER) oxidoreductase (show HSD17B6 Proteins) Ero1-L alpha and effectors modulating peroxisome proliferator-activated receptor gamma (PPAR gamma (show PPARG Proteins)) and SIRT1 (show SIRT1 Proteins) activities regulate secretion of adiponectin (show ADIPOQ Proteins) from 3T3-L1 adipocytes.

  10. These data shed new light on how the CHOP (show DDIT3 Proteins) pathway of apoptosis triggers calcium-dependent apoptosis through an ERO1-alpha-IP3R (show ITPR1 Proteins) pathway.

Pig (Porcine) ERO1-Like (S. Cerevisiae) (ERO1L) interaction partners

  1. Tissue distribution analysis of Ero1L and ERp44 (show ERP44 Proteins) genes revealed extremely high expression in adipose tissue, and the topology of their phylogenic tree indicates a high degree of conservation among different species.

ERO1-Like (S. Cerevisiae) (ERO1L) Protein Profile

Protein Summary

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.

Gene names and symbols associated with ERO1L

  • ERO1-like (ero1l)
  • ERO1-like (S. cerevisiae) (ERO1L)
  • ERO1-like beta (ero1lb)
  • ERO1-like (S. cerevisiae) (Ero1l)
  • ERO1-like (S. cerevisiae) (ero1l)
  • ERO1-alpha protein
  • ERO1-L protein
  • ERO1A protein
  • ero1l protein
  • ero1lb protein
  • zgc:63959 protein

Protein level used designations for ERO1L

ERO1-L-alpha , ERO1-like beta , ERO1-like protein alpha , Endoplasmic oxidoreductin-1-like protein , Oxidoreductin-1-L-alpha , ERO1-like (S. cerevisiae) , ERO1-L , endoplasmic oxidoreductin-1-like protein , oxidoreductin-1-L-alpha , endoplasmic reticulum oxidation 1 , endoplasmic reticulum oxidoreductin-1-like protein , global ischemia-induced protein 11

GENE ID SPECIES
446754 Xenopus laevis
452908 Pan troglodytes
548812 Xenopus (Silurana) tropicalis
100583502 Nomascus leucogenys
30001 Homo sapiens
50527 Mus musculus
171562 Rattus norvegicus
100125317 Bos taurus
100192435 Sus scrofa
393321 Danio rerio
423585 Gallus gallus
490691 Canis lupus familiaris
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