Abstract: The present invention provides purified and isolated polynucleotide sequences encoding a novel macrophage-derived C—C chemokine designated “Macrophage Derived Chemokine” (MDC), and polypeptide fragments and analogs thereof. Also provided are materials and methods for the recombinant or synthetic production of the chemokine, fragments, and analogs; and purified and isolated chemokine protein, and polypeptide fragments and analogs thereof. Also provided are antibodies reactive with the chemokine and methods of making and using all of the foregoing. Also provided are assays for identifying modulators of MDC chemokine activity.

Abstract: The present invention provides purified and isolated polynucleotide sequences encoding a novel human macrophage-derived C-C chemokine designated Macrophage Derived Chemokine (MDC), and polypeptide analogs thereof Also provided are materials and methods for the recombinant production of the chemokine, and purified and isolated chemokine protein, and polypeptide analogs thereof. Also provided are antibodies reactive with the chemokine and methods of making and using all of the foregoing.

Abstract: Amplified expression of recombinant DNA products is achieved in hosts expressing proteases that cleave at multi-basic amino acid residues. To this end, cDNAs encoding granulocyte-macrophage colony stimulating factor (GM-CSF) are mutated such that one or both of the arginine residues at positions 23 and 24 of the protein product are deleted or replaced by non-basic amino acid residues. The GM-CSF analogs thus obtained maintain the activity of the wild-type protein.

Abstract: Amplified expression of recombinant DNA products is achieved in hosts expressing proteases that cleave at multi-basic amino acid residues. To this end, cDNAs encoding granulocyte-macrophage colony stimulating factor (GM-CSF) are mutated such that one or both of the arginine residues at positions 23 and 24 of the protein product are replaced by non-basic amino acid residues. The GM-CSF analogs thus obtained maintain the activity of the wild-type protein.

Abstract: Amplified expression of recombinant DNA products is achieved in hosts expressing protease that cleave at multi-basic amino acid residues. To this end, wild-type genes encoding the desired protein products are mutated by substituting codons or eliminating codons encoding multi-basic amino acid residues while maintaining the activity of the expressed protein product. Mutation of the desired gene can be conveniently carried out by site-specific in vitro mutagenisis.