Wnt-1 belongs to the Wnt family of secreted glycoproteins inducing an intracellular signaling pathway involved in cell proliferation, differentiation and pattern formation. The canonical is one of three known branches. This is also valid in vitro and Wnts can be considered beneficial for culturing primary cells from organs provided Wnts are available and applicable even with cells of different species. It was shown here that internally c-myc-tagged murine Wnt-1 produced in the heterologous host Escherichia coli was appropriate for inducing intracellular signaling of the canonical Wnt pathway in eukaryotic cells via stabilization of cytosolic beta catenin. The pioneering injection of the protein into the blastocoels of Xenopus laevis embryos led to axis duplication and suppression of head formation. Applying the recombinant murine Wnt-1 to metanephric mesenchyme activated the tubulogenetic program. The signal inducing activity of the recombinant protein was also positively demonstrated in the TOPflash reporter assay. Although Wnts were recently purified from the growth media of stably transfected eukaryotic cell lines, it has reportedly never been successful to produce active Wnt proteins in pro- or eukaryotic microorganisms. Here soluble production in Escherichia coli and translocation into the oxidizing environment of the periplasm was achieved. The protein was purified using the internal c-myc-tag. The effect on the eukaryotic cells implies that activity was retained. Thus, this approach could make recombinant murine Wnt-1 available as a good starting point for also other Wnts needed for example for maintaining and differentiating stem cells, organ restoration therapy and tissue engineering.