Recombinant murine GM-CSF from E. coli has biological activity and is neutralized by a specific antiserum.

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Abstract
We report the production and characterization of a mouse granulocyte‐macrophage colony stimulating factor (mGM‐CSF) made in Escherichia coli. The synthesis of mGM‐CSF was directed by a plasmid containing a gene isolated from the EL‐4 cell line. After induction of expression and accumulation of the protein in E. coli, mGM‐CSF accounted for 10% of total cellular protein. This recombinant mGM‐CSF was purified to 90% homogeneity by chaotrope extraction and gel filtration. Recombinant mGM‐CSF, like the native molecule, stimulates the growth of granulocyte and macrophage colonies in serum‐free cultures of mouse bone marrow cells. Antibodies raised against recombinant mGM‐CSF not only reacted with the recombinant protein but also neutralized the biological activity of both native and recombinant mGM‐CSF. These results indicate that the functional structure of the recombinant protein is similar to that of native mGM‐CSF.