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     The image is immunohistochemistry of paraffin-embedded Human liver cancer tissue using P06410(EDEM1 Antibody) at dilution 1/20. (Original magnification: ×200)    

  
  

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     The image is immunohistochemistry of paraffin-embedded Human gastric cancer tissue using P06410(EDEM1 Antibody) at dilution 1/20. (Original magnification: ×200)    

  
  

The EDEM1 (ER degradation-enhancing alpha-mannosidase-like protein 1) antibody is a tool used to study a key player in endoplasmic reticulum (ER)-associated degradation (ERAD), a quality control pathway that targets misfolded glycoproteins for proteasomal degradation. EDEM1. a member of the glycosyl hydrolase 47 family, lacks enzymatic activity but acts as a lectin-like chaperone to recognize and direct improperly folded glycoproteins for ERAD. It facilitates the removal of terminally misfolded proteins by extracting them from the calnexin/calreticulin folding cycle and promoting their retrotranslocation to the cytosol via interactions with ERAD machinery components like SEL1L and HRD1.

Research suggests EDEM1 specifically trims mannose residues on N-linked glycans, marking substrates for degradation. Its expression is upregulated during ER stress through the unfolded protein response (UPR), linking it to cellular stress adaptation. Antibodies against EDEM1 are widely used in studies of protein quality control, ER stress-related diseases (e.g., neurodegenerative disorders, diabetes), and cancer biology. Common applications include Western blotting, immunofluorescence, and co-immunoprecipitation to investigate EDEM1 localization, protein interactions, or expression dynamics under stress conditions. Validation often involves knockout cell lines to confirm specificity. Commercial EDEM1 antibodies are typically raised against conserved regions (e.g., N-terminal residues 1-300) in hosts like rabbit or mouse.