Synonyms	Endoplasmic Reticulum Resident Protein 27;ER Protein 27;ERp27;ERP27;C12orf46
Species	Human
Expression_host	HEK293 Cells
Sequence	Glu26-Pro269
Accession	Q96DN0
Mol_Mass	53.7 kDa
Tag	C-mFc

Properties

Purity	> 84 % as determined by reducing SDS-PAGE.
Endotoxin level	< 1.0 EU per μg of the protein as determined by the LAL method.
Storage	Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.
Shipping	This product is provided as lyophilized powder which is shipped with ice packs.
Formulation	Lyophilized from sterile PBS, pH 7.4 Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the printed manual.
Reconstitution	Please refer to the printed manual for detailed information.

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.

Citations

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