Green fluorescent protein (GFP) is commonly used as a reporter protein in a wide range of biological experiments. The efficient protocol of Agrobacterium-mediated transient expression in Nicotiana excelsior was applied for quick preparative production of recombinant GFP. The protein purification scheme has been developed and included ammonium sulfate precipitation and Q-sepharose anion-exchange chromatography. It results in obtaining of a fraction with about 85% GFP homogeneity and the protein yield of about 75%.