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Intrinsically disordered proteins (IDPs) serve myriad regulatory functions in cells across the kingdoms of life, many of which are associated with collective properties of ensembles of IDPs such as liquid-liquid phase separation (LLPS) and formation of chemically-specific compartments. Recombinantly expressed, engineered IDPs have been explored for a wide range of bioanalytical applications including preparative and analytical separations. We focus on the use of one particular class of IDPs –the elastin-like polypeptides (ELPs) and their fusion proteins—as a particularly useful bioanalytical reagents. ELPs exhibit lower critical solubility temperatures in aqueous and their temperature-triggered LLPS can be easily tuned, predicted and exploited in a wide variety of applications. We have developed ELPs for biodetection applications in which the LLPS behavior of these IDPs are used either in sample preparation (extraction, preconcentration) or transduction of biomolecular recognition. This talk will present our fundamental studies of LLPS of ELPs as a model class of recombinant engineered IDPs, the use of ELPs in extraction of medically important bioanalytes from complex samples, and the use of ELPs in the formation of molecular assemblies that change their visual properties in the presence of important biomarkers (transduction). Emphasis is on development of bioanalytical methods that enable low cost, point-of-care, medical diagnostics.