ERO1L Polyclonal antibody

ERO1L Polyclonal Antibody for WB, IHC, ELISA

Host / Isotype

Rabbit / IgG

Reactivity

human, mouse, rat and More (1)

Applications

WB, IHC, IF, ELISA

Conjugate

Unconjugated

Cat no : 12007-1-AP

Synonyms

ERO1 alpha, ERO1 L, ERO1 L alpha, ERO1 like (S. cerevisiae), ERO1 like protein alpha, ERO1L, Oxidoreductin 1 L alpha



Tested Applications

Positive WB detected inmouse ovary tissue, A431 cells
Positive IHC detected inhuman pancreas cancer tissue
Note: suggested antigen retrieval with TE buffer pH 9.0; (*) Alternatively, antigen retrieval may be performed with citrate buffer pH 6.0

Recommended dilution

ApplicationDilution
Western Blot (WB)WB : 1:200-1:1000
Immunohistochemistry (IHC)IHC : 1:50-1:500
It is recommended that this reagent should be titrated in each testing system to obtain optimal results.
Sample-dependent, Check data in validation data gallery.

Product Information

12007-1-AP targets ERO1L in WB, IHC, IF, ELISA applications and shows reactivity with human, mouse, rat samples.

Tested Reactivity human, mouse, rat
Cited Reactivityhuman, mouse, rat, pig
Host / Isotype Rabbit / IgG
Class Polyclonal
Type Antibody
Immunogen ERO1L fusion protein Ag2620
Full Name ERO1-like (S. cerevisiae)
Calculated Molecular Weight 468 aa, 54 kDa
Observed Molecular Weight 54 kDa
GenBank Accession NumberBC008674
Gene Symbol ERO1L
Gene ID (NCBI) 30001
RRIDAB_10666441
Conjugate Unconjugated
Form Liquid
Purification MethodAntigen affinity purification
Storage Buffer PBS with 0.02% sodium azide and 50% glycerol pH 7.3.
Storage ConditionsStore at -20°C. Stable for one year after shipment. Aliquoting is unnecessary for -20oC storage. 20ul sizes contain 0.1% BSA.

Background Information

ERO1L, also named as ERO1-alpha, is an essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. It acts by oxidizing directly P4HB/PDI isomerase through a direct disulfide exchange. It 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. Glutathione may be required to regulate its activity in the endoplasmic reticulum. It may be responsible for a significant proportion of reactive oxygen species (ROS) in the cell, thereby being a source of oxidative stress. It is 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. This antibody has no cross reaction to ERO1.

Protocols

Product Specific Protocols
WB protocol for ERO1L antibody 12007-1-APDownload protocol
IHC protocol for ERO1L antibody 12007-1-APDownload protocol
FC protocol for ERO1L antibody 12007-1-APDownload protocol
Standard Protocols
Click here to view our Standard Protocols

Publications

SpeciesApplicationTitle
humanWB

Cancers (Basel)

ER Stress Response and Induction of Apoptosis in Malignant Pleural Mesothelioma: The Achilles Heel Targeted by the Anticancer Ruthenium Drug BOLD-100

Authors - Elia Ranzato
mouseWB

Cell Calcium

Mannan-binding lectin deficiency augments hepatic endoplasmic reticulum stress through IP3R-controlled calcium release.

Authors - Yu Chen
pigWB

J Virol

Porcine circovirus 2 manipulates PERK-ERO1α axis of endoplasmic reticulum in favor of its replication by derepressing viral DNA from HMGB1 sequestration within nuclei.

Authors - Renjie Sun
mouseWB

J Toxicol

Oxidative Stress and the ER Stress Response in a Murine Model for Early-Stage Alcoholic Liver Disease.

Authors - Galligan James J JJ
mouseWB,IF

Brain Res

Role of Ero1α in cognitive impairment induced by chronic hypoxia

Authors - Nan Zhang
ratWB

Transplantation

Protective Effect of Calpain Inhibition During Cold Ischemia on Ischemia-reperfusion Injury After Lung Transplantation

Authors - Yuuki Matsui