Cloning and expression of the human erythropoietin gene

F K Lin, S Suggs, C H Lin, J K Browne, R Smalling, J C Egrie, K K Chen, G M Fox, F Martin, Z Stabinsky, F K Lin, S Suggs, C H Lin, J K Browne, R Smalling, J C Egrie, K K Chen, G M Fox, F Martin, Z Stabinsky

Abstract

The human erythropoietin gene has been isolated from a genomic phage library by using mixed 20-mer and 17-mer oligonucleotide probes. The entire coding region of the gene is contained in a 5.4-kilobase HindIII-BamHI fragment. The gene contains four intervening sequences (1562 base pairs) and five exons (582 base pairs). It encodes a 27-amino acid signal peptide and a 166-amino acid mature protein with a calculated Mr of 18,399. The erythropoietin gene, when introduced into Chinese hamster ovary cells, produces erythropoietin that is biologically active in vitro and in vivo.

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