ERP44抗体

+ +

•  

   

     Gel: 8%SDS-PAGE, Lysate: 40 μg, Lane 1-7: A431 cells, K562 cells, 231 cells, HepG2 cells, Hela cells, A549 cells, Raji cells, Primary antibody: P12349(ERP44 Antibody) at dilution 1/200, Secondary antibody: Goat anti rabbit IgG at 1/8000 dilution, Exposure time: 10 seconds    

  
  

•  

   

     The image is immunohistochemistry of paraffin-embedded Human liver cancer tissue using P12349(ERP44 Antibody) at dilution 1/20. (Original magnification: ×200)    

  
  

•  

   

     The image is immunohistochemistry of paraffin-embedded Human colorectal cancer tissue using P12349(ERP44 Antibody) at dilution 1/20. (Original magnification: ×200)    

  
  

ERP44 (Endoplasmic Reticulum Protein 44 kDa) is a chaperone protein predominantly located in the endoplasmic reticulum (ER), playing a critical role in protein quality control and redox homeostasis. As a member of the protein disulfide isomerase (PDI) family, it facilitates disulfide bond formation, rearrangement, and structural stabilization of nascent glycoproteins, particularly those requiring precise folding for secretion. ERP44 is unique for its pH-sensitive cysteine-rich domain, enabling it to act as a calcium-regulated ER lumenal sensor. It interacts with client proteins such as IgM, adiponectin, and Ero1α, ensuring their proper maturation or retention until folding is complete.

ERP44 antibodies are essential tools for studying ER stress, unfolded protein response (UPR), and secretory pathway dynamics. They enable detection of ERP44 expression levels in various physiological and pathological contexts, including cancer, neurodegenerative diseases, and metabolic disorders. Commercial ERP44 antibodies are typically validated for applications like Western blotting, immunofluorescence, and immunoprecipitation, often targeting conserved regions across species (e.g., human, mouse, rat). Research using these antibodies has highlighted ERP44's dual role in promoting cell survival under stress and triggering apoptosis when protein misfolding is irreversible, underscoring its therapeutic relevance in diseases linked to ER dysfunction.