This review describes the different microtechniques developed for the extraction and purification of amyloid proteins from small specimens of fresh and formalin fixed tissues. These procedures differ with respect to solvent type, extraction conditions, and protein purification strategy. The advantages and disadvantages of the different microtechniques are discussed by taking into consideration tissue type (fresh of fixed) and size, amyloid type, and its content in the tissue. The review demonstrates the applicability of these techniques for the immunochemical and chemical characterisation of amyloid in different clinical forms of amyloidosis and in experimental small animal models. The clinical value of the applied microtechniques and their importance in the study of the pathogenesis of amyloid related diseases are outlined.