Spider silk is a natural product showing outstanding properties. High tensile strength and elasticity are attributed by the proteins major ampullate spidroin 1 (MaSp1) and Flag. The production of technical relevant amounts of these proteins by breeding and milking is not possible. One feasible solution is given by the production and purification of artificial spider silk proteins. In this work, the development of a purification method for two recombinant spider silk proteins (Q-MaSp1-100xELP, K-MaSp1-100xELP) is described. Following, the purification method was modified and used for the purification of 1xFlag-100xELP. The separation of contaminants was achieved applying a sequence of filtration and centrifugation steps, costly chromatographic steps could be avoided. Finally, 4 mg 1xFlag-100xELP, 273 mg K-MaSp1-100xELP and 413 mg Q-MaSP1-100xELP were purified.