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. Primary antibodies are available purified, or with a selection of fluorescent CF® Dyes and other labels. CF® Dyes offer exceptional brightness and photostability. Note: Conjugates of blue fluorescent dyes like CF®405S and CF®405M are not recommended for detecting low abundance targets, because blue dyes have lower fluorescence and can give higher non-specific background than other dye colors.