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.

Codice: PKSH030673_100μg | Marca: Elabscience | Confezionamento: 100μg

Specie: Human
Dettagli prodotto
  • Codice: PKSH030673_100μg
  • Marca: Elabscience
  • Specie target: Human
  • Host: HEK293 Cells
  • Confezionamento: Lyophilized from sterile PBS, pH 7.4<br/>Normally 5% - 8% trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization.<br/>Please refer to the specific buffer information in the printed manual.
  • Link: Apri link
  • Stoccaggio: 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.
  • Ig target: C12orf46;ER Protein 27;ERP27;ERp27;Endoplasmic Reticulum Resident Protein 27
  • Area di ricerca: Signal Transduction;