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- Li Xu
- *Sea Lane Biotechnologies, 1455 Adams Drive, Suite 2060, Menlo Park, CA 94025; and
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- Helena Yee
- *Sea Lane Biotechnologies, 1455 Adams Drive, Suite 2060, Menlo Park, CA 94025; and
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- Christina Chan
- *Sea Lane Biotechnologies, 1455 Adams Drive, Suite 2060, Menlo Park, CA 94025; and
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- Arun K. Kashyap
- *Sea Lane Biotechnologies, 1455 Adams Drive, Suite 2060, Menlo Park, CA 94025; and
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- Lawrence Horowitz
- *Sea Lane Biotechnologies, 1455 Adams Drive, Suite 2060, Menlo Park, CA 94025; and
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- Michael Horowitz
- *Sea Lane Biotechnologies, 1455 Adams Drive, Suite 2060, Menlo Park, CA 94025; and
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- Ramesh R. Bhatt
- *Sea Lane Biotechnologies, 1455 Adams Drive, Suite 2060, Menlo Park, CA 94025; and
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- Richard A. Lerner
- Department of Chemistry, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037
書誌事項
- 公開日
- 2008-08-05
- DOI
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- 10.1073/pnas.0805293105
- 公開者
- Proceedings of the National Academy of Sciences
この論文をさがす
説明
<jats:p> A unique type of combinatorial protein libraries has been constructed. These libraries are based on the pre-B cell receptor (pre-BCR). The pre-BCR is a protein that is produced during normal development of the antibody repertoire. Unlike that of canonical antibodies, the pre-BCR subunit is a trimer that is composed of an antibody heavy chain paired with two surrogate light chain (SLC) components. Combinatorial libraries based on these pre-BCR proteins in which diverse heavy chains are paired with a fixed SLC were expressed in mammalian, <jats:italic>Escherichia coli</jats:italic> , and phagemid systems. These libraries contain members that have nanomolar affinity for antigen. We term this type of antigen-binding protein a “surrobody” to distinguish it from the canonical antibody molecule. </jats:p>
収録刊行物
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- Proceedings of the National Academy of Sciences
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Proceedings of the National Academy of Sciences 105 (31), 10756-10761, 2008-08-05
Proceedings of the National Academy of Sciences