Rabbit anti-PDI - SPC-114C
|Product Name ||PDI Antibody|
|Catalog # ||SPC-114C|
|Package size ||25ul|
|Alternate Product Sizes ||SPC-114D|
|Datasheet ||SPC 114 Protein Disulphide Isomerase (PDI) Organlle Marker|
|Research Area ||Chaperones, Organelle Markers|
|Alternative Names ||PDA2, PDI, PDIA2, PDIP, pancreatic protein disulfide isomerase|
|Clone Number ||N/A|
|Host Species ||Rabbit|
|Immunogen ||Rat PDI synthetic peptide conjugated to KLH|
|Applications ||WB, IP, ICC, IHC|
|Species Reactivity ||Human, Mouse, Rat, Dog, Hamster, Monkey, Guinea pig, Bovine, Sheep, Pig, Xenopus|
|Accession Number ||NP_001099245.2|
|Gene ID ||287164|
|Background Info ||Detects ~58kDa|
|Recommended Dilutions ||1:4000 (WB)|
|Form ||Rabbit antiserum|
|Storage Buffer ||Rabbit antiserum|
|Certificate of Analysis ||A 1:4000 dilution of SPC-114 was sufficient for detection of PDI in 20μg of HeLa cell lysate by ECL immunoblot analysis.|
|Storage Temp ||-20 °C|
|Shipping Temp ||Blue Ice or 4 °C|
|Research 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.
|Cited References ||1. Priscilla T.Y. Leunga, Yu Wangb, Sarah S.T. Maka, W.C. Nga, Kenneth M.Y. Leung. Differential proteomic responses in hepatopancreas and adductor muscles of the green-lipped mussel Perna viridis to stresses induced by cadmium and hydrogen peroxide. Aquatic Toxicology Volume 105, Issues 1-2, September 2011, Pages 49-61. doi:10.1016/j.aquatox.2011.05.010|