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ERO1L Products

Antibodies
Lysates
ERO1L Overexpression Lysate
ERO1L Overexpression Lysate
NBP2-07312
Species: Hu
Applications: WB
Proteins
Recombinant Human ERO1L alpha ...
Recombinant Human ERO1L alpha Prot...
9855-EO
Species: Hu
Applications: Enzyme Activity
Formulation Catalog # Availability Price  
Recombinant Human ERO1L His P ...
Recombinant Human ERO1L His Protein
NBP2-51682
Species: Hu
Applications: PAGE
ERO1L Recombinant Protein Ant ...
ERO1L Recombinant Protein Antigen
NBP1-84799PEP
Species: Hu
Applications: AC

Description

Perhaps the most distinctive feature of protein folding in the ER is the abundance of disulfide bonds that must form during maturation of proteins traveling along the secretory pathway. Formation of disulfide bonds is a redox reaction. Thus, to match the flux of disulfide bonds that exit from the ER by virtue of protein secretion, a flux of oxidizing equivalents into the ER is required. In eukaryotic cells, the essential protein relay supporting this flux, and hence disulfide bond formation, involves endoplasmic reticulum oxidoreductin 1 (Ero1) and protein disulfide isomerase (PDI). The temporal pattern of hypoxic ERO1-L alpha induction is very similar to that of genes triggered by the hypoxia inducible transcription factor (HIF-1) and is characteristically mimicked by cobalt and by deferoxamine, but is absent in cells with a defective aryl hydrocarbon receptor translocator (ARNT, HIF-1 alpha). We speculate from these findings that the expression of ERO1-L alpha is probably regulated via the HIF-pathway and thus belongs to the family of classic oxygen regulated genes.

Bioinformatics

Entrez Rat
Human
Mouse
Uniprot Human
Human
Human
Product By Gene ID 30001
Alternate Names
  • EC 1.8.4
  • EC 1.8.4.-
  • Endoplasmic oxidoreductin-1-like protein
  • ERO1 (S. cerevisiae)-like
  • ERO1A
  • ERO1-alpha
  • ERO1-L
  • ERO1-L-alpha
  • ERO1-like (S. cerevisiae)
  • ERO1-like protein alpha
  • Oxidoreductin-1-L-alpha
  • oxidoreductin-1-L-alpha

Research Areas for ERO1L

Find related products by research area and learn more about each of the different research areas below.

Cancer
ER Markers
Hypoxia
Membrane Trafficking and Chaperones
Signal Transduction

Related ERO1L Blog Posts

Check out the latest blog posts on ERO1L.
ERO1 Activity: A Potential Source of ER-Derived Oxidative Stress.
Disulfide bond formation is a pivotal step in the maturation and release of secretory proteins that are controlled by specific endoplasmic reticulum (ER) resident enzymes. An important element in this process is ERO (ER oxidoreduction), a glycosylated...    Read more.
Read more ERO1L related blogs.