Protein disulfide isomerase (PDI) is a multifunctional enzyme belonging to the thioredoxin superfamily, primarily located in the endoplasmic reticulum (ER). It plays a critical role in catalyzing the formation, breakage, and rearrangement of disulfide bonds during protein folding, ensuring proper tertiary structure and functional maturation of nascent polypeptides. Beyond its chaperone activity, PDI participates in ER stress responses, calcium homeostasis, and redox signaling. Dysregulation of PDI has been implicated in various pathologies, including neurodegenerative diseases (e.g., Alzheimer’s and Parkinson’s), cancer metastasis, and cardiovascular disorders, where disrupted protein folding contributes to cellular dysfunction.
PDI antibodies are essential tools for studying its expression, localization, and mechanistic roles in health and disease. They enable detection of PDI in techniques like Western blotting, immunohistochemistry, and immunofluorescence, aiding research on ER stress pathways or protein misfolding. Some studies also explore PDI as a therapeutic target, with antibodies designed to modulate its activity in pathological contexts. However, challenges remain in distinguishing PDI from its isoforms (e.g., PDIA1-PDIA6) due to structural similarities, necessitating careful antibody validation. Overall, PDI antibodies bridge fundamental research and translational applications, offering insights into protein quality control mechanisms and potential therapeutic strategies.