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A Convenient and General Expression Platform for the Production of Secreted Proteins from Human Cells
Published on: July 31, 2012
High-level production of recombinant immunoglobulins in mammalian cells
1IDEC Pharmaceuticals Corporation, San Diego.
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.
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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