Anti-Protein Disulfide Isomerase (PDI) Antibody

This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. Receptor for LGALS9; the interaction retains P4HB at the cell surface of Th2 T helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration. {UniProtKB:P07237}.

Western blot: Use at 1:4,000 dilution. A band of approx. 58 kD is detected.Immunocytochemistry/Immunohisto- chemistry: Use at 2-5 ug/ml. <br><br>Immunoprecipitation: Use at 10 ug/ml.

Store frozen product at or below -20°C. For optimal storage, aliquot to smaller portions and store at -20°C to -70°C. Avoid repeated freeze/thaw cycles.

A microsomal enzyme known as Protein Disulfide Isomerase (PDI) is involved in the formation of disulfide bonds in many extracellular proteins through its oxidase and isomerase activities. It is also involved in the reduction of disulfide bonds in proteins. PDI is located primarily in the endoplasmic reticulum (ER) but may also be found in the cytosol. PDI can reside in the ER due to the highly conserved KDEL sequence at its carboxy terminus which serves as an ER-retention signal.