The HSPE1 antibody targets Heat Shock Protein Family E (Hsp10) member 1. a mitochondrial chaperonin critical for protein folding and assembly. HSPE1. also known as HSP10. forms a complex with HSP60 to facilitate proper folding of nascent mitochondrial proteins, ensuring cellular homeostasis under stress. This antibody is widely used in techniques like Western blotting, immunohistochemistry, and immunofluorescence to study HSPE1 expression and localization. Research links HSPE1 dysregulation to pathologies including cancer, neurodegenerative disorders, and autoimmune diseases. In tumors, elevated HSPE1 levels are associated with proliferation and therapy resistance, serving as a potential biomarker. Conversely, impaired HSPE1 function may contribute to protein aggregation in Alzheimer’s or Parkinson’s disease. Additionally, HSPE1 autoantibodies have been detected in rheumatoid arthritis, suggesting its role in autoimmune responses. Structurally, HSPE1 contains conserved heat shock domains enabling its chaperone activity. Antibodies against HSPE1 help elucidate its dual role in cytoprotection and disease pathogenesis, offering insights into therapeutic targeting. Their specificity (monoclonal/polyoclonal) determines applications in mechanistic studies or diagnostic assays. Overall, HSPE1 antibodies are vital tools for exploring mitochondrial stress responses and disease mechanisms. (Word count: 199)