Sample Research Paper

Purification of hybrid-hybridoma antibodies is still labour-intensive and expensive, although some progress has been made. Chemical linkage of F(ab´) fragments requires enzymic digestion of whole antibodies, which may be affected by the antibody isotype, and may furthermore vary from antibody to antibody.

Recombinant Bispecific antibodies can be successfully produced in various expression systems. Although each protein may reveal characteristic expression problems due to its unique amino acid sequence, some general schemes emerge from today’s experience in the literature. While bacterial expression offers the potential for large yields, difficult refolding procedures may be required to obtain functional proteins. Today, production in Escherichia coli is most commonly used for the Bispecific (dibody) format, while short-chain Bispecific antibodies are preferentially expressed in mammalian cells. Interesting novel expression systems include yeast or insect cells, as well as transgenic plants or animals. For the production of clinical-grade material, however, these later systems are less well defined regarding potentially dangerous contaminants and furthermore differ substantially from mammalian cells with respect to their glycosylation pattern. Purification of recombinant Bispecific antibodies can be achieved by several well-defined affinity tags, such as polyhistidine or strep. These tags further have the issues of immunogenicity, but they can be taken care of with further research.

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