Heat shock protein 10 (HSP10), also known as HSPE1 or chaperonin 10. is a member of the heat shock protein family, which plays critical roles in cellular stress responses and protein homeostasis. As a co-chaperone, HSP10 forms a functional complex with HSP60 in the mitochondrial matrix, assisting in the folding of newly synthesized or denatured proteins. This HSP60/HSP10 chaperonin system is essential for maintaining mitochondrial proteostasis and energy metabolism.
Antibodies targeting HSP10 are widely used in research to investigate its expression, localization, and interaction with HSP60 in both physiological and pathological contexts. Studies have linked altered HSP10 levels to various diseases, including cancer, neurodegenerative disorders (e.g., Alzheimer's), and autoimmune conditions. In cancer, elevated HSP10 expression has been observed in tumors like colorectal and breast cancers, suggesting potential roles in cell proliferation and apoptosis regulation. HSP10 antibodies enable detection via techniques such as Western blotting, immunohistochemistry, and immunofluorescence.
Interestingly, HSP10 may also exhibit extracellular roles in immune modulation, with implications for inflammatory diseases. Commercially available HSP10 antibodies are typically validated for specificity across human, mouse, and rat samples, supporting cross-species studies. Ongoing research continues to explore HSP10's dual functions as a molecular chaperone and disease biomarker, driving demand for reliable antibodies in mechanistic and diagnostic investigations.