Abstract
Recombinant proteins expressed in bacteria are sometimes insoluble, aggregated, and incorrectly folded. For those Src homology 2 (SH2) domains that are insoluble in bacteria, baculovirus-insect cell expression systems can be an alternative to produce soluble and functionally active proteins. We describe a protocol for cloning and purification of GST-tagged SH2 domains using the Bac-to-Bac baculovirus expression system.
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Acknowledgment
We thank Joshua Jadwin and Silas Khong Ng for assistance with editing the manuscript, and Bruce Mayer for his continuous encouragement and support. This study was partly supported by grant CA1154966 from the National Institutes of Health and Quest for CURES (QFC) grant from the Leukemia and Lymphoma Society (to K.M.).
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Ogiue-Ikeda, M., Machida, K. (2017). Expression and Purification of SH2 Domains Using Baculovirus Expression System. In: Machida, K., Liu, B. (eds) SH2 Domains. Methods in Molecular Biology, vol 1555. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-6762-9_11
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DOI: https://doi.org/10.1007/978-1-4939-6762-9_11
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Publisher Name: Humana Press, New York, NY
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Online ISBN: 978-1-4939-6762-9
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