Membrane proteins perform important tasks like communication and transport in and between single cells. Cells that lack functional membrane proteins will cease to work properly, resulting in a variety of human diseases. Membrane protein research is thus a necessity for the progress of developing medical treatment. Synthetic production of membrane proteins could replace the demanding task of protein extraction from cells. In vitro protein synthesis describes the process of protein expression without living cells. Supplementing the reaction with membranes leads to integration of the proteins into them, so providing a minimal cell membrane model consisting of a membrane with embedded protein. Yet, it is not clear how this integration process occurs. Establishment of reproducible methods for in vitro protein expression and detection is critical for research in this field. The choice of expression system, among many available, and the design of a suitable expression vector are the first steps towards successful in vitro protein synthesis. From available eukaryotic systems, one derived from wheat germ was chosen due to its comparatively low levels of contaminating messenger RNA. Protein detection with Western blot has proven to be inadequate in this case, as the specificity of most antibodies used is not high enough and multiple reaction components interfered with the desired binding events. The incorporation of fluorophore-labelled lysine into the proteins produced in the in vitro synthesis reaction seems to be a more suitable method. Reproducible expression and detection of the AIDS-related protein CD4 was achieved this way.