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SDS-PAGE

ERP27 recombinant protein

Recombinant Human ERP27 Protein (Fc tag)

Gene Names
ERP27; PDIA8; C12orf46
Purity
> 84 % as determined by SDS-PAGE
Synonyms
ERP27; Recombinant Human ERP27 Protein (Fc tag); C12orf46 ERP27; ERP27 recombinant protein
Ordering
For Research Use Only!
Host
Human Cells
Purity/Purification
> 84 % as determined by SDS-PAGE
Form/Format
Lyophilized from sterile PBS, pH 7.4
Sequence Length
172
Application Notes
The recombinant human ERP27/mFc is a disulfide-linked homodimer. The reduced monomer comprises 478 amino acids and has a predicted molecular mass of 53.7 kDa. The apparent molecular mass of the protein is approximately 59 in SDS-PAGE under reducing conditions due to glycosylation.
Predicted N Terminal
Glu 26
Endotoxin
< 1.0 EU per mug of the protein as determined by the LAL method
Preparation and Storage
Samples are stable for up to twelve months from date of receipt at -70 degree C

SDS-PAGE

SDS-PAGE
Related Product Information for ERP27 recombinant protein
Background: ERP27 contains 1 thioredoxin domain and is a noncatalytic member of the protein disulfide isomerase family. Protein disulfide isomerases (PDIs) constitute a family of structurally related enzymes which catalyze disulfide bonds formation, reduction, or isomerization of newly synthesized proteins in the lumen of the endoplasmic reticulum (ER). They act also as chaperones, and are, therefore, part of a quality-control system for the correct folding of the proteins in the same subcellular compartment. PDI has been found to have moderate effects (25-fold) on the rate of oxidative folding of proteins in vitro. Recombinant Human Protein Disulfide Isomerase is involved in disulphide-bond formation and isomerization, as well as the reduction of disulphide bonds in proteins. Recombinant PDI has been found to have moderate effects (25-fold) on the rate of oxidative folding of proteins in vitro. ERP27 is a widely expressed protein which localizes to the ER and may act as a protease, protein disulfide isomerase, thiol-disulfide oxidase or phospholipase. ERP27 doesn't contain a CXXC active site motif indicating that it is a catalytically redox-inactive member of the protein disulfide isomerase family.

Description: A DNA sequence encoding the human ERP27 (Q96DN0) (Glu26-Pro269) was fused with Fc region of mouse IgG at the C-terminus.

NCBI and Uniprot Product Information

NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Accession #
Molecular Weight
30,480 Da
NCBI Official Full Name
endoplasmic reticulum resident protein 27 isoform 2
NCBI Official Synonym Full Names
endoplasmic reticulum protein 27
NCBI Official Symbol
ERP27
NCBI Official Synonym Symbols
PDIA8; C12orf46
NCBI Protein Information
endoplasmic reticulum resident protein 27
UniProt Protein Name
Endoplasmic reticulum resident protein 27
UniProt Gene Name
ERP27
UniProt Synonym Gene Names
C12orf46; ER protein 27; ERp27

NCBI Description

This gene encodes a noncatalytic member of the protein disulfide isomerase (PDI) family of endoplasmic reticulum (ER) proteins. The canonical protein has an N-terminal signal sequence, two thioredoxin (TRX)-like domains and a C-terminal ER-retention sequence. Alternative splicing results in multiple transcript variants encoding distinct isoforms; some of which lack domains present in the canonical protein. [provided by RefSeq, Dec 2016]

Uniprot Description

ERP27: Belongs to the protein disulfide isomerase family. Interacts with PDIA3. Binds somatostatin-14 via hydrophobic interactions

Protein type: Secreted; Secreted, signal peptide

Chromosomal Location of Human Ortholog: 12p12.3

Cellular Component: endoplasmic reticulum

Molecular Function: protein binding; protein disulfide isomerase activity

Biological Process: protein folding

Research Articles on ERP27

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Product Notes

The ERP27 erp27 (Catalog #AAA2545347) is a Recombinant Protein produced from Human Cells and is intended for research purposes only. The product is available for immediate purchase. The recombinant human ERP27/mFc is a disulfide-linked homodimer. The reduced monomer comprises 478 amino acids and has a predicted molecular mass of 53.7 kDa. The apparent molecular mass of the protein is approximately 59 in SDS-PAGE under reducing conditions due to glycosylation. Researchers should empirically determine the suitability of the ERP27 erp27 for an application not listed in the data sheet. Researchers commonly develop new applications and it is an integral, important part of the investigative research process. It is sometimes possible for the material contained within the vial of "ERP27, Recombinant Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.

Precautions

All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.

Disclaimer

Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.

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