BD Transduction Laboratories™ Purified Mouse Anti-PDI
Clone 34/PDI (RUO)
Western blot analysis of PDI on HCT-8 cell lysate. Lane 1: 1:250, lane 2: 1:500, lane 3: 1:1000 dilution of anti-PDI.
Western blot analysis of PDI on HCT-8 cell lysate. Lane 1: 1:250, lane 2: 1:500, lane 3: 1:1000 dilution of anti-PDI.
Preparation And Storage
Recommended Assay Procedures
Western blot: Please refer to http://www.bdbiosciences.com/pharmingen/protocols/Western_Blotting.shtml
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
- Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
- Source of all serum proteins is from USDA inspected abattoirs located in the United States.
The ER is the site of translation of membrane and secretory proteins. Following synthesis, it shuttles these proteins through a contiguous membrane system to their appropriate destinations. Protein disulfide isomerase (PDI) is an abundant, multifunctional, eukaryotic protein. Although it exhibits ubiquitous expression, it is primarily located in the ER lumen. Here, it functions to catalyze the isomerization of intramolecular disulfide bridges, thereby allowing them to generate their most thermodynamically stable configurations. This role in rearrangement has lead to the classification of PDI as a chaperone. Although protein folding occurs in its absence, PDI may be essential for it to proceed at a physiological relevant rate. In addition, PDI is the β-subunit of prolyl 4- hydroxylase and is a component of the triglyceride transfer complex. PDI is retained in the ER lumen via its C-terminal -KDEL sequence. Via this sequence, it is continuously recycled back to the ER from other membranous compartments. Thus, PDI is a diverse protein whose primary function may be to correct disulfide bonding and, thus, ensure the most stable conformation of newly synthesized proteins.
Development References (5)
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Jenne N, Frey K, Brugger B, Wieland FT. Oligomeric state and stoichiometry of p24 proteins in the early secretory pathway. J Biol Chem. 2002; 277(48):46504-46511. (Clone-specific: Western blot). View Reference
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Schlegel A, Arvan P, Lisanti MP. Caveolin-1 binding to endoplasmic reticulum membranes and entry into the regulated secretory pathway are regulated by serine phosphorylation. Protein sorting at the level of the endoplasmic reticulum. J Biol Chem. 2001; 276(6):4398-4408. (Clone-specific: Western blot). View Reference
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Weissman JS, Kim PS. Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase. Nature. 1993; 365(6442):185-188. (Biology). View Reference
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Wetterau JR, Combs KA, Spinner SN, Joiner BJ. Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex. J Biol Chem. 1990; 265(17):9800-9807. (Biology). View Reference
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Yamauchi K, Yamamoto T, Hayashi H. Sequence of membrane-associated thyroid hormone binding protein from bovine liver: its identity with protein disulphide isomerase. Biochem Biophys Res Commun. 1987; 146(3):1485-1492. (Biology). View Reference
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