For several years, it has been possible to detect typical extracellular matrix proteins (ECMs), such as osteopontin, osteonectin, and osteocalcin, in archaeological bone. Additionally, it has proven possible to detect growth factors and hormones (e.g., TGF-β, BMP-2, gonatropine), bone matrix proteins of the immune system (e.g., IgG, IgA, interleukine), and biomarker for diseases, such as tumor markers (e.g., PSA, PSA/ACT) or typical molecules characteristic for nonspecific infectious disease (e.g., TNF-α, IFN-γ) and specific infectious diseases (e.g., from Mycobacterium tuberculosis, Ag 85), in dry (macerated) bone. Now, we are able to detect these ECMs in fossil bone as well. Thus, evolutionarily old molecules, such as BMP-2, albumin, and matrix-gla-proteins (MPG), can be detected in fossil bone of various specimens (e.g., Anancus arvernensis) and compared to each other and to recent specimens. Furthermore, the bone matrix protein patterns of childhood and adulthood (at the date of death) in the same individual can be compared, providing us with information on changes of living conditions during the individual's lifetime. Finally, the future possibilities of the study of ECMs in fossil human species are briefly outlined.This contribution hopes to attract interest in newly available methods of biochemical and, in particular proteomic, research in paleoanthropology. These have potential to provide insights toward a better understanding of the evolution of mankind.