The ERO1A Polyclonal Antibody (PAC044634) is a valuable tool for researchers studying ERO1A, a key enzyme involved in oxidative protein folding in the endoplasmic reticulum. This antibody, raised in rabbits, is highly specific to human samples and has been validated for use in Western blot applications. By binding to the ERO1A protein, this antibody allows for accurate detection and analysis in various cell types, making it an essential reagent for studies in cell biology and protein folding mechanisms.ERO1A plays a crucial role in maintaining protein homeostasis by facilitating disulfide bond formation, which is essential for the correct folding of secretory and membrane proteins.
Dysregulation of ERO1A has been linked to various diseases such as cancer, neurodegenerative disorders, and metabolic syndromes, making it a promising therapeutic target for drug development. Understanding the function of ERO1A is essential for unraveling its role in protein folding pathways and its implications for disease pathogenesis.
Recombinant Human ERO1-like protein α protein (24-260AA)
Form:
Liquid
Storage Buffer:
PBS with 0.02% sodium azide, 50% glycerol, pH7.3.
Purification Method:
Antigen Affinity Purified
Clonality:
Polyclonal
Isotype:
IgG
Conjugate:
Non-conjugated
Western blot. All lanes: ERO1L antibody at 1.25µg/ml. Lane 1: A431 whole cell lysate. Lane 2: 293T whole cell lysate. Secondary. Goat polyclonal to rabbit IgG at 1/10000 dilution. Predicted band size: 54 kDa. Observed band size: 54, 25 kDa..
Immunohistochemistry of paraffin-embedded human pancreatic tissue using PACO44634 at dilution of 1:100.
Immunohistochemistry of paraffin-embedded human small intestine tissue using PACO44634 at dilution of 1:100.
Background:
Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. Required for the proper folding of immunoglobulins. Involved in 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. Plays an important role in ER stress-induced, CHOP-dependent apoptosis by activating the inositol 1,4,5-trisphosphate receptor IP3R1.
ERO1L: 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. Predominantly monomer. May function both as a monomer and a homodimer. Interacts with PDILT. Stimulated by hypoxia; suggesting that it is regulated via the HIF-pathway. Widely expressed at low level. Expressed at high level in upper digestive tract. Highly expressed in esophagus. Weakly expressed in stomach and duodenum. Enzyme activity is tightly regulated to prevent the accumulation of reactive oxygen species in the endoplasmic reticulum. Reversibly down-regulated by the formation of disulfide bonds between the active site Cys-94 and Cys-131, and between Cys- 99 and Cys-104. Glutathione may be required to regulate its activity in the endoplasmic reticulum. Belongs to the EROs family.
UniProt Protein Details:
Protein type:EC 1.8.4.-; Oxidoreductase; Secreted; Secreted, signal peptide
Molecular Function:disulfide oxidoreductase activity; oxidoreductase activity; protein binding; protein disulfide isomerase activity; protein disulfide oxidoreductase activity
Biological Process: chaperone cofactor-dependent protein folding; protein folding; protein modification process; release of sequestered calcium ion into cytosol; response to reactive oxygen species; response to temperature stimulus
