Target Protein Insolubility

Robust expression of recombinant protein in microorganisms often results in some fraction of the protein being produced in an insoluble, inactive form. For example, proteins originating from higher organisms may be insoluble due to differences in translation rate, redox potential and chaperone or cofactor availability. There are many possible solutions to this problem including lowering the inducer concentration, reducing the induction temperature and testing alternative expression hosts. However, successful production of recombinant protein may require expression of the target as a fusion to a solubility partner. Over the last three decades many solubility partners have been employed and maltose binding protein (MBP) remains as one of the most effective at enhancing the expression level and solubility of fused target proteins.

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    Publications related to Target Protein Insolubility
    • Agrawal, A., Bisharyan, Y., Papoyan, A, Bednenko, J., Cardarelli, J., Yao, M., Clark, T., Berkm​en, M., Ke, N., Colussi, P. (2019) Fusion to Tetrahymena thermophila granule lattice protein 1 confers solubility to sexual stage malaria antigens in Escherichia coli. Protein Expr Purif; 153, 7-17. PubMedID: 30081196, DOI: 10.1016/j.pep.2018.08.001.
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