HSP60抗体

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     Red: Control Antigen (100ng); Purple: Antigen (10ng); Green: Antigen (50ng); Blue: Antigen (100ng);    

  
  

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     Western blot analysis using HSP60 mouse mAb against T47D (1), Hela (2), HepG2 (3), A549 (4), Jurkat (5), HEK293 (6), NIH/3T3 (7), PC-12 (8) and Cos7 (9) cell lysate.    

  
  

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     Immunofluorescence analysis of 3T3-L1 cells using HSP60 mouse mAb (green). Blue: DRAQ5 fluorescent DNA dye. Red: Actin filaments have been labeled with Alexa Fluor-555 phalloidin.    

  
  

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     Flow cytometric analysis of Hela cells using HSP60 mouse mAb (green) and negative control (purple).    

  
  

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     Immunohistochemical analysis of paraffin-embedded human lung cancer tissues (left) and kidney cancer tissues (right) using HSP60 mouse mAb with DAB staining.    

  
  

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     Immunohistochemical analysis of paraffin-embedded human breast cancer tissues (left) and colon cancer tissues (right) using HSP60 mouse mAb with DAB staining.    

  
  

Heat shock protein 60 (HSP60), a member of the chaperonin family, is a highly conserved mitochondrial protein involved in protein folding, assembly, and stress response. Under physiological conditions, HSP60 assists in maintaining cellular homeostasis by ensuring proper protein conformation. However, dysregulation or abnormal exposure of HSP60 can trigger immune responses, leading to the production of anti-HSP60 antibodies. These antibodies are implicated in various autoimmune and inflammatory diseases, including rheumatoid arthritis, type 1 diabetes, and atherosclerosis. Molecular mimicry between bacterial HSP60 (e.g., from *Chlamydia pneumoniae* or *Helicobacter pylori*) and human HSP60 is thought to contribute to cross-reactive antibody production, potentially driving tissue damage.

In cancer, HSP60 overexpression in tumors may promote cell survival, while circulating anti-HSP60 antibodies have been explored as diagnostic or prognostic biomarkers. However, their role remains controversial, as both protective and pathogenic effects have been reported depending on context. Research also links HSP60 autoantibodies to neurodegenerative disorders like Alzheimer’s disease, possibly due to stress-induced chaperone release. Despite clinical associations, challenges persist in distinguishing pathogenicity from incidental immune reactivity. Studies using HSP60 antibodies as research tools or therapeutic targets continue to advance understanding of its dual roles in cellular stress and disease.