Oxidoreductase-protein disulfide isomerase (PDI) is a homodimer consisting of subunits that catalyzes thiol-disulfide exchange, mediates folding of newly synthesized proteins and functions as a molecular chaperone. PDI localizes to the lumen of the endoplasmic reticulum (ER), where in conjunction with folding-helper proteins, such as immunoglobulin heavy chain binding protein (BiP), mediates tertiary and quaternary protein-processing. Cell surface PDI induces sulfhydryl-mediated conformational changes in integrin-mediated adhesion receptor-ligand interactions, thereby regulating integrin responses and cell adhesion. Additionally, PDI functions as a subunit of two more complex enzyme systems: the prolyl-4-hydroxylase and the triacylglycerol transfer proteins.
Background References
1. Obser T et al. Identification and characterization of the elusive mutation causing the historical von Willebrand Disease type IIC Miami. J Thromb Haemost 14:1725-35 (2016).
2. Koumangoye R & Delpire E The Ste20 kinases SPAK and OSR1 travel between cells through exosomes. Am J Physiol Cell Physiol 311:C43-53 (2016).
Sequence Similarity
Belongs to the protein disulfide isomerase family.
Western blot analysis of PDIA2 on different lysates with Rabbit anti-PDIA2 antibody (ET1702-70) at 1/1,000 dilution.
Lane 1: HEK-293 cell lysate (20 µg/Lane) Lane 2: NIH/3T3 cell lysate (20 µg/Lane) Lane 3: Human liver tissue lysate (40 µg/Lane)
Predicted band size: 92 kDa Observed band size: 92 kDa
Exposure time: Lane 1: 1 minute 18 seconds; Lane 2-3: 25 seconds; ECL: K1801;
4-20% SDS-PAGE gel.
Proteins were transferred to a PVDF membrane and blocked with 5% NFDM/TBST for 1 hour at room temperature. The primary antibody (ET1702-70) at 1/1,000 dilution was used in 5% NFDM/TBST at 4℃ overnight. Goat Anti-Rabbit IgG - HRP Secondary Antibody (HA1001) at 1/50,000 dilution was used for 1 hour at room temperature.
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