Description
Recombinant full-length human HSP60 was expressed in E. coli cells using a N-terminal GST tag.
Scientific Background: HSP60 is a chaperonin protein, required for ATP-dependent folding of precursor polypeptides and complex assembly and prevents aggregation and mediates protein refolding after heat shock. Mutations and variations in the HSP 60 gene product may be implicated in genetic diseases (1). HSP60 has been strongly implicated as an example of molecular mimicry in the pathogenicity of autoimmune diseases in T cell-mediated protection. Human HSP60 was found to activate the complement system in normal human serum in a dose-dependent manner. Since complement activation plays an important role in the development of atherosclerosis, the levels of complement-activating anti-HSP60 antibodies are elevated in atherosclerosis-related diseases. (2)