**Background of ERP29 Antibody**
ERP29 (Endoplasmic Reticulum Protein 29 kDa), also known as ERp29. is a conserved protein disulfide isomerase (PDI)-like chaperone predominantly localized in the endoplasmic reticulum (ER). Unlike classical PDIs, ERP29 lacks a catalytic thioredoxin domain but retains structural homology, featuring two domains: a conserved N-terminal thioredoxin-like domain and a C-terminal α-helical domain. It plays a critical role in protein folding, quality control, and secretory pathway regulation, facilitating the maturation and transport of client proteins, including hormones (e.g., thyroglobulin) and membrane receptors.
ERP29 is implicated in cellular stress responses, acting as a molecular chaperone to mitigate ER stress by assisting in the correct folding of nascent proteins. Its expression is regulated by the unfolded protein response (UPR) and varies across tissues, with high levels observed in secretory cells. Dysregulation of ERP29 has been linked to diseases such as cancer, where it exhibits dual roles—acting as a tumor suppressor (e.g., in breast and prostate cancers) or promoter (e.g., in lung cancer), depending on context. It also associates with neurodegenerative disorders, potentially influencing aggregation-prone protein handling.
ERP29 antibodies are essential tools for studying its expression, localization, and interaction networks. They enable detection in immunofluorescence, Western blotting, and immunohistochemistry, aiding research into ER stress mechanisms, cancer biology, and therapeutic targeting.