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 (1). This process is called oxidative protein folding. Disulfide isomerase (PDI) has two thioredoxin homology domains and catalyzes the formation and isomerization of these disulfide bonds (2). Other ER resident proteins that possess the thioredoxin homology domains, including endoplasmic reticulum stress protein 72 (ERp72), constitute the PDI family (3,4). ERp72 contains three thioredoxin homology domains (3) and plays a role in the formation and isomerization of disulfide bonds on secretory proteins (3,4).
Applications:
Suitable for use in Western Blot. Other applications not tested.
Recommended Dilution:
Western Blot: 1:1000
Optimal dilutions to be determined by the researcher.
Storage and Stability:
May be stored at 4 degrees C for short-term only. For long-term storage, aliquot and store at -20 degrees C. Aliquots are stable for at least 12 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
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