PDCA5 (Protein Disulfide Isomerase A5), also known as PDIA5 or P5. is a member of the protein disulfide isomerase (PDI) family, which plays critical roles in oxidative protein folding within the endoplasmic reticulum (ER). These enzymes catalyze the formation, isomerization, and reduction of disulfide bonds during protein maturation. PDIA5 contains thioredoxin-like domains with a CXXC active site motif, enabling its redox activity. Unlike classical PDIs (e.g., PDIA1), PDIA5 lacks a C-terminal ER retention signal and may localize to both the ER and other cellular compartments, suggesting broader functional versatility.
Studies indicate PDIA5 participates in ER stress responses, apoptosis regulation, and quality control of secreted/membrane proteins. It interacts with key chaperones like BiP/GRP78 and modulates the unfolded protein response (UPR). Dysregulation of PDIA5 has been linked to diseases such as cancer, neurodegenerative disorders, and diabetes, where disrupted protein homeostasis contributes to pathogenesis.
PDIA5 antibodies are essential tools for detecting PDIA5 expression, localization, and interaction partners in research. They enable investigations into its role in cellular stress pathways, disease mechanisms, and potential therapeutic targeting. Commercial antibodies are typically validated in applications like Western blotting, immunofluorescence, and immunoprecipitation, though cross-reactivity with other PDI family members should be cautiously evaluated. Recent research also explores PDIA5's extracellular roles in thrombus formation and immune regulation, expanding its biological significance.