*Optimal dilutions/concentrations should be determined by the researcher.
Not tested in other applications.
HCT116 , MCF-7 , mouse stomach
Rat, Bovine, Pig, Rhesus Monkey(>80% identity)
0.1M Tris, 0.1M Glycine, 10% Glycerol (pH7). 0.01% Thimerosal was added as a preservative.
Store as concentrated solution. Centrifuge briefly prior to opening vial. For short-term storage (1-2 weeks), store at 4ºC. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.
0.95 mg/ml (Please refer to the vial label for the specific concentration.)
Recombinant protein encompassing a sequence within the center region of human ERO1L. The exact sequence is proprietary.
Purified by antigen-affinity chromatography.
For laboratory use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.
endoplasmic reticulum oxidoreductase 1 alpha , ERO1-L , ERO1-L-alpha , ERO1-alpha , ERO1L , ERO1LA , Ero1alpha
Endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side
Essential 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.