Technical Data
P3122-11
PDI (Protein Disulfide Isomerase)
Description:
Secretory proteins translocate into the endoplasmic reticulum (ER) after their synthesis where they are post-translationally modified and properly folded. To reach their native conformation, many secretory proteins require the formation of intra- or inter-molecular disulfide bonds. This process is called oxidative protein folding. Disulfide isomerase (PDI) catalyzes the formation and isomerization of these disulfide bonds. Studies on mechanisms of oxidative folding suggest that molecular oxygen oxidizes ER-protein Ero1, which in turn oxidizes PDI through disulfide exchange. This event is then followed by PDI-catalyzed disulfide bond formation on folding proteins.

Applications:
Suitable for use in Western Blot, Immunofluorescence, Immunocytochemistry and Immunohistochemistry. Other applications not tested.

Recommended Dilutions:
Western Blot: 1:1000
Immunohistochemistry (Paraffin): 1:100. Antigen retrieval in citrate buffer required.
Immunofluorescence (IF-IC): 1:50; Requires methanol permeabilization.
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20C. Aliquots are stable for 12 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
TypeIsotypeCloneGrade
PabIgGAffinity Purified
SizeStorageShippingSourceHost
100ul-20CBlue IceHumanRabbit
Concentration:
Not determined
Immunogen:
Synthetic peptide corresponding to residues surrounding Pro329 of human PDI.
Purity:
Purified by Protein A and peptide affinity chromatography.
Form
Supplied as a liquid in 10mM sodium HEPES, pH 7.5, 150mM sodium chloride, 0.1mg/ml BSA, 50% glycerol.
Specificity:
Recognizes endogenous levels of total human PDI protein at ~57kD. Species Crossreactivity: monkey, mouse and rat.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Huppa, J.B. & Ploegh, H.L., Cell 92: 145-148 (1998). 2. Ellgaard, L. & Ruddock, L.W., EMBO Rep. 6: 28-32 (2005). 3. Tu, B.P. & Weissman, J.S., J. Cell Biol. 164: 341-346 (2004).