Full length recombinant human protein was used as the immunogen for the HSP60 antibody.
The heat shock proteins (HSPs) comprise a group of highly conserved, abundantly expressed proteins with diverse functions, including the assembly and sequestering of multiprotein complexes, transportation of nascent polypeptide chains across cellular membranes, and the regulation of protein folding. The mitochondrial and cytosolic localization of HSP60, combined with its binding and catalysis of folding of newly synthesized proteins destined for the mitochondrial matrix, classify this protein as a molecular chaperone. An additional role of HSP 60 is to act as a cell surface marker for T cell recognition, as well as being involved in a danger signal cascade immune response. HSP60 has been shown to influence apoptosis in tumor cells, and changes in its expression level may serve as a biomarker, as down-regulated HSP60 expression indicates a poor prognosis as well as a risk of tumor infiltration development, especially with regard to urothelial carcinomas. In ovarian cancer, decreased expression of HSP60 correlates with aggressive tumor types, while overexpression is correlated with a better patient prognosis.
