Since its first production from muscle tissue more than 65 years ago, our knowledge about actin has come a long way. While at the beginning it was identified as a muscle protein, nowadays actin is considered as one of the most important components of the cytoskeleton, playing a crucial role in cell motility, adhesion, morphology and intracellular transport processes. In vitro models have been constructed for about 20 years to gain better insight into the chemophysical and biomechanical properties of actin networks by being able to reduce and tune its complexity. The complexity of these models ranges from single actin filaments (F-actin) in interaction with actin-associated molecules and proteins, F-actin network gels to F-actin loaded vesicles to freely suspended F-actin networks in microfluidic environments. This review summarizes the development of F-actin network models and highlights their applicability towards step-by-step construction of complex cortex mimicking systems.