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• W2805295087 abstract "The Brevibacillus expression system has been successfully employed for the efficient productions of a variety of recombinant proteins, including enzymes, cytokines, antigens and antibody fragments. Here, we succeeded in secretory expression of Trastuzumab Fab antibody fragments using B. choshinensis/BIC (Brevibacillus in vivocloning) expression system. In the fed-batch high-density cell culture, recombinant Trastuzumab Fab with amino-terminal His-tag (His-BcFab) was secreted at high level, 1.25 g/liter, and Fab without His-tag (BcFab) at ∼145 mg/L of culture supernatant. His-BcFab and BcFab were purified to homogeneity using combination of conventional column chromatographies with a yield of 10-13%. This BcFab preparation exhibited native structure and functions evaluated by enzyme-linked immunosorbent assay, surface plasmon resonance, circular dichroism measurements and size exclusion chromatography. To our knowledge, this is the highest production of Fab antibody fragments in gram-positive bacterial expression/secretion systems." @default.
• W2805295087 created "2018-06-13" @default.
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• W2805295087 date "2018-10-01" @default.
• W2805295087 modified "2023-10-13" @default.
• W2805295087 title "Efficient production of Trastuzumab Fab antibody fragments in Brevibacillus choshinensis expression system" @default.
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• W2805295087 doi "https://doi.org/10.1016/j.pep.2018.05.013" @default.
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