Overview

Description

  • NatureRecombinant
  • SourceEscherichia coli
  • Amino Acid Sequence
    • AccessionQ96HE7
    • SpeciesHuman
    • Molecular weight18 kDa
    • Amino acids37 to 189
    • TagsHis-DHFR tag N-Terminus

Specifications

Our Abpromise guarantee covers the use of ab125981 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Applications

    SDS-PAGE

  • FormLyophilised
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Store at -20ºC.

    Constituents: 0.32% Tris HCl, 0.58% Sodium chloride

  • ReconstitutionReconstitute with water to desired concentration.

General Info

  • Alternative names
    • Endoplasmic oxidoreductin 1 like protein
    • Endoplasmic oxidoreductin-1-like protein
    • Endoplasmic reticulum oxidoreductin 1-like
    • ERO1 alpha
    • ERO1 L
    • ERO1 Lalpha
    • ERO1 like protein alpha
    • ERO1-alpha
    • ERO1-L
    • ERO1-L-alpha
    • ERO1-like (S. cerevisiae)
    • ERO1-like alpha
    • ERO1-like protein alpha
    • ERO1-like, S. cerevisiae, homolog of, alpha
    • ERO1A
    • ERO1A_HUMAN
    • ERO1L
    • ERO1LA
    • Oxidoreductin 1 Lalpha
    • Oxidoreductin-1-L-alpha
    • PRO865
    • UNQ434
    see all
  • FunctionEssential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly P4HB/PDI isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on P4HB/PDI to transfer oxidizing equivalent. Associates with ERP44 but not with GRP54, demonstrating that it does not oxidize all PDI related proteins and can discriminate between PDI and related proteins. Its reoxidation probably involves electron transfer to molecular oxygen via FAD. Acts independently of glutathione. May be responsible for a significant proportion of reactive oxygen species (ROS) in the cell, thereby being a source of oxidative stress. Required for the folding of immunoglobulin proteins. Responsible for the release of the unfolded cholera toxin from reduced P4HB/PDI in case of infection by V.cholerae, thereby playing a role in retrotranslocation of the toxin.
  • Tissue specificityWidely expressed at low level. Expressed at high level in upper digestive tract. Highly expressed in esophagus. Weakly expressed in stomach and duodenum.
  • Sequence similaritiesBelongs to the EROs family.
  • Post-translational
    modifications
    N-glycosylated.
    The Cys-94/Cys-99 and Cys-394/Cys-397 disulfide bonds constitute the redox-active center. The Cys-94/Cys-99 disulfide bond may accept electron from P4HB and funnel them to the active site disulfide Cys-394/Cys-397.
  • Cellular localizationEndoplasmic reticulum membrane. The association with ERP44 is essential for its retention in the endoplasmic reticulum.
  • Information by UniProt

References for Recombinant Human ERO1L protein (ab125981)

ab125981 has not yet been referenced specifically in any publications.

Product Wall

There are currently no Abreviews or Questions for ab125981.
Please use the links above to contact us or submit feedback about this product.

Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"