Product Name	PDI Antibody
Catalog #	SPC-114C
Package size	25ul

Alternate Product Sizes	SPC-114D
Type	Polyclonal
Conjugate	N/A
Datasheet	SPC 114 Protein Disulphide Isomerase (PDI) Organlle Marker
Description	Anti-PDI
Research Area	Chaperones, Organelle Markers
Alternative Names	PDA2, PDI, PDIA2, PDIP, pancreatic protein disulfide isomerase
Clone Number	N/A
Host Species	Rabbit
Isotype	N/A
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
SwissProt	P04785
Background Info	Detects ~58kDa
Recommended Dilutions	1:4000 (WB)
Form	Rabbit antiserum
Storage Buffer	Rabbit antiserum
Concentration	N/A
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