Production of engineered IgM-binding single-chain antibodies inEscherichia coli
| Autor: | James Nagle, Michele L. Rollence, Steven W. Dodd, Paul L. Hallberg, Mark S. Oelkuct, David Filpula, Timothy K. Lee |
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| Rok vydání: | 1995 |
| Předmět: |
Lymphokines
Base Sequence biology medicine.drug_class Molecular Sequence Data Antibodies Monoclonal Prostatic Secretory Proteins Bioengineering IgM binding Immunoglobulin light chain Monoclonal antibody Applied Microbiology and Biotechnology Primary and secondary antibodies Molecular biology Recombinant Proteins J chain Antibody Specificity Complementary DNA Escherichia coli biology.protein medicine Amino Acid Sequence Antibody Single-Chain Antibodies Biotechnology |
| Zdroj: | Journal of Industrial Microbiology. 14:371-376 |
| ISSN: | 1476-5535 0169-4146 |
| DOI: | 10.1007/bf01569953 |
| Popis: | Two single-chain antibodies were engineered and tested as novel binding proteins with specificity for immunoglobulin M. Genes for the two single-chain Fv proteins were assembled from the variable light chain cDNA and variable heavy chain cDNA of monoclonal antibodies DA4.4 and Bet 2, which specifically bind human IgM and mouse IgM, respectively. Both single-chain Fv proteins were designed with a 14-amino acid linker which bridged the variable light chain and variable heavy chain domains. The two proteins were expressed in Escherichia coli, purified and assayed for IgM-binding activity. Both proteins demonstrate a binding specificity for their corresponding IgM which is similar to the monoclonal antibodies from which they were derived. These small IgM-binding proteins may have applications in the investigation of the immune response and in the detection and purification of monoclonal antibodies, cell-associated antibodies, and IgM from serum. |
| Databáze: | OpenAIRE |
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