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Cat. Number
069554417000227
Chemical Name
PDI Polyclonal Antibody
References
Synonyms
  • Protein Disulphide Isomerase
Stability 1 year
Storage -20°C
Shipping Wet ice in continental US; may vary elsewhere
Specificity
Human PDI +
Mouse PDI +
Rat PDI +
Canine PDI +
Hamster PDI +
Monkey PDI +
Guinea pig PDI +
Bovine PDI +
Ovine PDI +
Procine PDI +
Xenopus PDI +
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Background Reading

Yoshimori, T., Semba, T., Takemoto, H., et al. Protein disulfide-isomerase in rat exocrine pancreatic cells is exported from the endoplasmic reticulum despite possessing the retention signal. J Biol Chem 265(26) 15984-15990 (1990).

Schultz-Norton, J.R., McDonald, W.H., Yates, J.R., et al. Protein disulfide isomerase serves as a molecular chaperone to maintain estrogen receptor α structure and fuction. Mol Endocrinol 20(9) 1982-1995 (2006).

Delom, F., Mallet, B., Carayon, P., et al. Role of extracellular molecular chaperones in the folding of oxidized proteins. Refolding of colloidal thyroglobulin by protein disulfide isomerase and immunoglobulin heavy chain-binding protein. J Biol Chem 276(24) 21337-21342 (2001).

Mater, M., Kies, U., Kammermeier, R., et al. BiP and PDI cooperate in the oxidative folding of antibodies in vitro. J Biol Chem 275(38) 29421-29425 (2000).

Na, K.S., Park, B.C., Jang, M., et al. Protein disulfide isomerase is cleaved by caspase-3 and -7 during apoptosis. Mol Cells 24(2) 261-267 (2007).

Janiszewski, M., Lopes, L.R., Carmo, A.O., et al. Regulation of NAD(P)H oxidase by associated protein disulfide isomerase in vascular smooth muscle cells. J Biol Chem 280(49) 40813-40819 (2005).

Turano, C., Coppari, S., Altieri, F., et al. Proteins of the PDI family: Unpredicted non-ER locations and functions. J Cell Physiol 193(2) 154-163 (2002).

Show all 7 Hide all but first 3
Size Global Purchasing
25 µL  
100 µL  

Description

Antigen: synthetic peptide from rat PDI conjugated to KLH · Host: rabbit · Application(s): WB, IP, ICC, and IHC · 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 disulphite 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 55 kDa protein located primarily in the ER, however studies have also proved its presence in the cytosol.6 PDI has the ability to reside in the ER permanently due to the highly conserved KDEL sequence at its carboxy-terminus.7 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.8

1 Prada, J.A.H., Ferreira, A.J., Katovich, M.J., et al. Structure-based identification of small-molecule angiotensin-converting enzyme 2 activators as novel antihypertensive agents. Hypertension 51 1312-1317 (2008).

2 Mater, M., Kies, U., Kammermeier, R., et al. BiP and PDI cooperate in the oxidative folding of antibodies in vitro. J Biol Chem 275(38) 29421-29425 (2000).

3 Delom, F., Mallet, B., Carayon, P., et al. Role of extracellular molecular chaperones in the folding of oxidized proteins. Refolding of colloidal thyroglobulin by protein disulfide isomerase and immunoglobulin heavy chain-binding protein. J Biol Chem 276(24) 21337-21342 (2001).

4 Schultz-Norton, J.R., McDonald, W.H., Yates, J.R., et al. Protein disulfide isomerase serves as a molecular chaperone to maintain estrogen receptor α structure and fuction. Mol Endocrinol 20(9) 1982-1995 (2006).

5 Turano, C., Coppari, S., Altieri, F., et al. Proteins of the PDI family: Unpredicted non-ER locations and functions. J Cell Physiol 193(2) 154-163 (2002).

6 Na, K.S., Park, B.C., Jang, M., et al. Protein disulfide isomerase is cleaved by caspase-3 and -7 during apoptosis. Mol Cells 24(2) 261-267 (2007).

7 Janiszewski, M., Lopes, L.R., Carmo, A.O., et al. Regulation of NAD(P)H oxidase by associated protein disulfide isomerase in vascular smooth muscle cells. J Biol Chem 280(49) 40813-40819 (2005).

8 Yoshimori, T., Semba, T., Takemoto, H., et al. Protein disulfide-isomerase in rat exocrine pancreatic cells is exported from the endoplasmic reticulum despite possessing the retention signal. J Biol Chem 265(26) 15984-15990 (1990).

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