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     The image is immunohistochemistry of paraffin-embedded Human cervical cancer tissue using P09635(ERP27 Antibody) at dilution 1/35. (Original magnification: ×200)    

  
  

The ERP27 antibody targets ERP27 (Endoplasmic Reticulum Protein 27), a protein implicated in endoplasmic reticulum (ER)-associated processes, particularly protein folding and quality control. ERP27. also known as ERp27 or PDIA8. belongs to the protein disulfide isomerase (PDI) family, though it lacks the catalytic thioredoxin-like domains found in classical PDIs. It is structurally characterized by two non-catalytic thioredoxin-fold domains and a C-terminal ER-retention motif (KDEL), which anchors it within the ER lumen. ERP27 is proposed to act as a molecular chaperone or co-factor, assisting in the oxidative folding of nascent glycoproteins by stabilizing transient folding intermediates or facilitating interactions with other PDI family members, such as ERp57.

Studies suggest ERP27 plays a role in cellular stress responses, including the unfolded protein response (UPR), by modulating ER homeostasis. Its expression is upregulated under conditions of ER stress, such as nutrient deprivation or hypoxia, highlighting its importance in maintaining proteostasis. ERP27 antibodies are widely used in research to investigate ER stress mechanisms, protein misfolding diseases (e.g., neurodegenerative disorders, diabetes), and cancer biology, where dysregulated ER function is often observed. These antibodies enable detection of ERP27 via techniques like Western blotting, immunofluorescence, and co-immunoprecipitation, aiding in elucidating its interactions and regulatory pathways. Further research aims to clarify its precise molecular functions and therapeutic potential in ER-related pathologies.