The PDIA6 antibody targets Protein Disulfide Isomerase A6 (PDIA6), a member of the protein disulfide isomerase (PDI) family primarily involved in oxidative protein folding within the endoplasmic reticulum (ER). PDIA6 facilitates the formation, isomerization, and reduction of disulfide bonds, ensuring proper tertiary structure of nascent proteins. Structurally, it contains thioredoxin-like domains with catalytic CGHC motifs critical for its redox activity. Beyond folding, PDIA6 participates in ER stress response, calcium homeostasis, and cell signaling. Dysregulation of PDIA6 has been linked to pathologies such as cancer, neurodegenerative disorders, and cardiovascular diseases, where its overexpression or dysfunction impacts cell survival, metastasis, or protein aggregation. PDIA6 antibodies are essential tools for studying its expression, localization, and mechanistic roles in these contexts. They are widely used in techniques like Western blotting, immunohistochemistry, and immunofluorescence to explore PDIA6's interaction with client proteins or its modulation under stress conditions. Additionally, these antibodies aid in evaluating PDIA6 as a potential therapeutic target or biomarker in disease models. Research continues to uncover its extra-ER roles, including extracellular redox signaling in thrombosis and inflammation, highlighting the antibody's versatility in both basic and translational studies.