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|Tested species reactivity||Human, Mouse, Rat|
|Host / Isotype||Rabbit / IgG|
|Immunogen||Synthetic peptide made the the N-terminal region of the human protein.|
|Purification||Antigen affinity chromatography|
|Storage buffer||BBS with 1% BSA|
|Storage Conditions||-20° C, Avoid Freeze/Thaw Cycles|
|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.
ERO1L (endoplasmic oxidoreductin-1-like protein) is localized in ER membrane as peripheral membrane protein on lumenal side, its association with ERP44 being essential for its retention in the ER, and is unique in coupleing oxygen reduction to de novo disulfides formation. ERO1L enzyme is broadly distributed at low levels in several tissues with highest levels in upper digestive tract especially the esophagus, and is stimulated by hypoxia via HIF-signaling. ERO1L generally exists as monomer, but has the ability to function as monomer or homodimer and interacts with PDILT. After translation, ERO1L gets n-glycosylated and the disulphide bonds constitute the redox-active center whereby the Cys-94/Cys-99 disulfide bond accept electron from P4HB followed by funneling the same to the active site disulfide Cys-394/Cys-397. ERO1L acts by oxidizing directly P4HB/PDI isomerase through direct disulfide exchange and can associates with ERP44. Its reoxidation probably involves electron transfer to molecular oxygen via FAD and acts independently of GSH. ERO1L is implicated in immunoglobulin folding, oxidative stress, release of unfolded cholera toxin from reduced P4HB/PDI upon Vibrio cholerae infection, and plays a key role in ER stress-induced CHOP-dependent apoptosis through inositol 1,4,5-trisphosphate receptor IP3R1 activation.
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; Global ischemia-induced protein 11; Oxidoreductin-1-L-alpha
ERO1-alpha; ERO1-L; ERO1-L-alpha; ERO1A; Ero1alpha; ERO1L; ERO1LA; Giig11; UNQ434/PRO865