Application
| WB, IHC, IP, ICC |
|---|---|
| Primary Accession | P04785 |
| Other Accession | NP_001099245.2 |
| Host | Rabbit |
| Reactivity | Human, Mouse, Rat, Hamster, Monkey, Pig, Bovine, Xenopus, Dog, Sheep, Guinea Pig |
| Clonality | Polyclonal |
| Description | Rabbit Anti-Rat PDI Polyclonal |
| Target/Specificity | Detects ~58kDa. |
| Other Names | PDA2 Antibody, PDI Antibody, PDIA2 Antibody, PDIP Antibody, pancreatic protein disulfide isomerase Antibody |
| Immunogen | Rat PDI synthetic peptide conjugated to KLH |
| Purification | Peptide Affinity Purified |
| Storage | -20ºC |
| Storage Buffer | PBS pH7.4, 50% glycerol, 0.09% sodium azide |
| Shipping Temperature | Blue Ice or 4ºC |
| Certificate of Analysis | A 1:1000 dilution of SPC-114 was sufficient for detection of PDI in 20 µg of HeLa cell lysate by ECL immunoblot analysis. |
| Cellular Localization | Endoplasmic Reticulum | Endoplasmic Reticulum Lumen |
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Provided below are standard protocols that you may find useful for product applications.
Background
The three dimensional structure of many extracellular proteins is stabilized by the formation of disulphide bonds. Studies suggest that a microsomal enzyme known as Protein Disulphide Isomerase (PDI) is involved in disulphide-bond formation via its oxidase activity and isomerization via its isomerase activity, as well as the reduction of disulphide bonds in proteins (1). Studies suggest BiP and PDI work together sequentially to increase oxidation of these proteins (2, 3). PDI has also been found to function as a chaperone to prevent the aggregation of unfolded substrates, and serves as a subunit of prolyl 4-hydroxylase and microsomal triglyceride transferase (4, 5). PDI is an abundant 55kDa protein located primarily in the ER, however studies have also proved its presence in the cytosol (1). PDI has the ability to reside in the ER permanently due to the highly conserved KDEL sequence at its carboxy-terminus (6). It uses carboxy-terminal KDEL as a retention signal, and this appears to be sufficient to reduce the secretion of proteins from the ER. This retention is reported to be mediated by a KDEL receptor (7).
References
1. NA K.S. et al. (2007) Mol Cells. 24(2): 261-7.
2. Mayer M., Kies U., Kammermeier R., and Buchner J. (2000) J Biol Chem. 275(38): 29421-5.
3. Delom F., Mallet B., Carayon P., and Lejeune P.J. (2001) J Biol Chem 276(24): 21337-42.
4. Schultz-Norton J.R., McDonald W.H., Yates J.R. and Nardulli A.M. (2006) Mol Endocrinol 20(9): 1982-95.
5. Turano C., Coppari S. Altieri F. and Ferraro (2002) J Cell Physiol 193: 154-163.
6. Janiszewski M. (2005) J. Biol Chem. 280(49): 40813- 40819.
7. Yoshimori T., et al. (1990) J Biol Chem. 265(26): 15984-90.