Invitrogen™ PDI Monoclonal Antibody (RL90)

Description

MA3-019 detects protein disulphide-isomerase (PDI) from human, rat, porcine and mouse tissues as well as hamster cells. MA3-019 has been successfully used in Western blot, immunofluorescence, immunohistochemical, flow cytometry, and immunoprecipitation procedures. By Western blot, this antibody detects a protein at 59 kDa representing PDI from rat liver extract or a slightly higher protein at 61 kDa representing PDI from human liver extract. Immunohistochemical staining of PDI in rat intestine with MA3-019 yields a pattern consistent with cytoplasmic staining. In immunoprecipitation procedures MA3-019 has been shown to inhibit the activity of PDI in vitro. MA3-019 has also been found to inhibit disulfide bond reduction of the HIV protein, gp120, at the cell surface of CHO cells and human lymphoid cells. In immunohistochemistry procedures, formalin-fixed paraffin-embedded tissue sections are recommended. The MA3-019 antigen is purified rat PDI.

Protein disulfide isomerase (PDI) is a multifunctional protein that catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, the protein seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. It may therefore cause structural modifications of exofacial proteins. Inside the cell, PDI seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, it functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, it facilitates aggregation (anti-chaperone activity). PDI may be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. It 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.