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|Tested species reactivity||Human, Mouse, Rat|
|Host / Isotype||Rabbit / IgG|
|Immunogen||A synthetic peptide made the the N-terminal region of the human protein.|
|Purification||Antigen affinity chromatography|
|Storage buffer||sodium borate with 1% BSA|
|Storage Conditions||4° C, store in dark|
|Tested Applications||Dilution *|
|Western Blot (WB)||1:1000-1:2000|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
This ERO1L antibody is useful for Western Blot, where a band ~57 kDa is observed.
Depending on the samples used ERO1L can also appear as a doublet which is believed to represent the oxidized and reduced forms of the protein.
Suggested positive control: 293T, INS-1, and MIN6 cell lysate.
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.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
endoplasmic oxidoreductin-1-like protein; endoplasmic reticulum oxidation 1; endoplasmic reticulum oxidoreductase alpha; endoplasmic reticulum oxidoreductin-1-like protein; ERO1-alpha; ERO1-L; ERO1-L-alpha; ERO1-like protein alpha; ERO1A; global ischemia-induced protein 11; oxidoreductin-1-L-alpha; UNQ434/PRO865
ERO1-alpha; ERO1-L; ERO1-L-alpha; ERO1A; Ero1alpha; ERO1L; ERO1LA; Giig11; UNQ434/PRO865