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AB180283

Recombinant Human ERO1L protein (His tag N-Terminus)

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Recombinant Human ERO1L protein (His tag N-Terminus) is a Human Full Length protein, in the 24 to 468 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE.

View Alternative Names

ERO1L, UNQ434/PRO865, ERO1A, ERO1-like protein alpha, ERO1-L, ERO1-L-alpha, Endoplasmic oxidoreductin-1-like protein, Endoplasmic reticulum oxidoreductase alpha, Oxidoreductin-1-L-alpha

1 Images
SDS-PAGE - Recombinant Human ERO1L protein (His tag N-Terminus) (AB180283)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human ERO1L protein (His tag N-Terminus) (AB180283)

15% SDS-PAGE analysis of ab180283 (3μg).

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

Q96HE7

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 10% Glycerol (glycerin, glycerine), 0.32% Tris HCl

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMGSEEQPPETAAQRCFCQVSGYLDDCTCDVETIDRFNNYRLFPRLQKLLESDYFRYYKVNLKRPCPFWNDISQCGRRDCAVKPCQSDEVPDGIKSASYKYSEEANNLIEECEQAERLGAVDESLSEETQKAVLQWTKHDDSSDNFCEADDIQSPEAEYVDLLLNPERYTGYKGPDAWKIWNVIYEENCFKPQTIKRPLNPLASGQGTSEENTFYSWLEGLCVEKRAFYRLISGLHASINVHLSARYLLQETWLEKKWGHNITEFQQRFDGILTEGEGPRRLKNLYFLYLIELRALSKVLPFFERPDFQLFTGNKIQDEENKMLLLEILHEIKSFPLHFDENSFFAGDKKEAHKLKEDFRLHFRNISRIMDCVGCFKCRLWGKLQTQGLGTALKILFSEKLIANMPESGPSYEFHLTRQEIVSLFNAFGRISTSVKELENFRNLLQNIH","proteinLength":"Full Length","predictedMolecularWeight":"54.4 kDa","actualMolecularWeight":null,"aminoAcidEnd":468,"aminoAcidStart":24,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q96HE7","tags":[{"tag":"His","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

ERO1L also known as ERO1-alpha is a protein involved in the formation of disulfide bonds in the endoplasmic reticulum important for protein folding. The molecular mass of ERO1L is approximately 54 kDa. ERO1L primarily expresses in tissues with high secretory activities such as the liver and pancreas. It plays a vital role in maintaining redox homeostasis within the cell by transferring electrons from protein disulfide isomerase to molecular oxygen.
Biological function summary

ERO1L contributes to oxidative protein folding within the endoplasmic reticulum. As part of a complex it interacts with protein disulfide isomerases to facilitate the introduction of disulfide bonds into nascent proteins. This function is essential for the proper maturation of secreted proteins influencing cellular protein management processes. ERO1L activity impacts cellular responses to stress and influences the capacity of cells to handle unfolded proteins.

Pathways

ERO1L significantly influences the protein folding and endoplasmic reticulum-associated degradation pathway. It has strong associations with protein disulfide isomerase and interacts within the unfolded protein response to manage cellular stress caused by misfolded proteins. The protein contributes to the maintenance of a stable internal environment during conditions where protein folding demands increase.

ERO1L shows connections to cancer and neurodegenerative disorders. Aberrant expression of ERO1L can influence tumor growth due to its role in modulating cellular stress responses and managing protein folding in cancer cells. The protein also shows a relationship with neurodegenerative conditions through its involvement in protein misfolding pathways which are critical in diseases like Alzheimer's. ERO1L collaborates with proteins like protein disulfide isomerase and participates in cellular mechanisms underlying these conditions.
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Specifications

Form

Liquid

Additional notes

ab180283 is purified using conventional chromatography techniques.

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General info

Function

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 (PubMed : 29858230). Plays an important role in ER stress-induced, CHOP-dependent apoptosis by activating the inositol 1,4,5-trisphosphate receptor IP3R1. 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.

Sequence similarities

Belongs to the EROs family.

Post-translational modifications

N-glycosylated.. The Cys-94/Cys-99 and Cys-394/Cys-397 disulfide bonds constitute the redox-active center. The Cys-94/Cys-99 disulfide bond may accept electron from P4HB and funnel them to the active site disulfide Cys-394/Cys-397 (By similarity). The regulatory Cys-99/Cys-104 disulfide bond stabilizes the other regulatory bond Cys-94/Cys-131 (PubMed:23027870).. Phosphorylated on Ser-145 by FAM20C in the Golgi which increases its enzymatic activity (PubMed:29858230). Phosphorylation is induced by lactation (By similarity). It is also induced by hypoxia and reductive stress (PubMed:29858230).

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Product protocols

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Target data

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 (PubMed : 29858230). Plays an important role in ER stress-induced, CHOP-dependent apoptosis by activating the inositol 1,4,5-trisphosphate receptor IP3R1. 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.
See full target information ERO1A
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