High-level production of recombinant immunoglobulins in mammalian cells.
Successful high-level expression of recombinant immunoglobulins has now been reported in several different types of mammalian cells. This has been achieved using random integration of immunoglobulin genes co-linked with a drug-resistance gene into cellular DNA. After gene integration, increases in immunoglobulin-gene expression are obtained by selection for increases in expression of the drug-resistance marker. Expression levels attained by this method are several fold higher than those produced by a good hybridoma. Soon, site-specific homologous recombination may replace random integration as the favored methodology for initial expression of all proteins in mammalian cells, including immunoglobulins.
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IDEC Pharmaceuticals Corporation, San Diego.
D000818:Animals; D001709:Biotechnology; D002478:Cells, Cultured; D005803:Genes, Immunoglobulin; D005822:Genetic Vectors; D006801:Humans; D007136:Immunoglobulins / Q000096:biosynthesis* / Q000235:genetics; D015202:Protein Engineering; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000235:genetics
D007136:Immunoglobulins; D011994:Recombinant Proteins