Heat-shock proteins (HSPs) are a group of proteins whose expression is increased when the cells are exposed to elevated temperatures or other stressful conditions. This increase in expression is transcriptionally regulated. The function of HSPs is similar in virtually all living organisms, from bacteria to humans. Their expression also occur under non-stressful conditions, simply 'monitoring' the cell's proteins, i.e., they carry old proteins to the cell's 'recycling bin' and they help newly synthesized proteins fold properly. These activities are part of a cell's own repair system. HSPs are molecular chaperones for protein molecules. They are usually cytoplasmic proteins and they perform functions in various intracellular processes. Tumour-derived HSP-peptide complexes (HSPPCs) can be used for vaccination against malignancies. In particular, HSPPC-96 complex, called Vitespen (formerly Oncophage) is a HSPs-based vaccine made from individual patients' tumours with a promising role in cancer management. This vaccine has been extensively studied in Phase I and II clinical trials, showing activity on different malignancies, including gastric cancer, colorectal cancer, pancreatic cancer, non-Hodgkin's lymphoma and chronic myelogenous leukaemia. The vaccine has also been studied in Phase III clinical trials in melanoma and kidney cancer, showing an excellent safety profile with essentially no toxicity. Thus, HSP-based vaccines are a novel therapeutic approach with a promising role in cancer management.