CrossRef Text and Data Mining
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Improving Soluble Expression of β-Galactosidase in Escherichia coli by Fusion with Thioredoxin
E. S. Nam, H. J. Jung, J. K. Ahn
Asian-Australas J Anim Sci. 2004;17(12):1751-1757.   Published online January 1, 2004

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Expression of canine parvovirus-β-galactosidase fusion proteins in Escherichia coli
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Production of human antimicrobial peptide LL-37 in Escherichia coli using a thioredoxin–SUMO dual fusion system
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Preparation of bioactive soluble human leukemia inhibitory factor from recombinant Escherichia coli using thioredoxin as fusion partner
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Thioredoxin fusion construct enables high-yield production of soluble, active matrix metalloproteinase-8 (MMP-8) in Escherichia coli
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Soluble expression of archaeal proteins in Escherichia coli by using fusion-partners
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Synthesis of 32P-labelled protein probes using a modified thioredoxin fusion protein expression system in Escherichia coli
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Heterologous expression and stability of the Escherichia coli β-galactosidase gene in Streptococcus lactis by translation fusion
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Expression and purification of bioactive soluble murine stem cell factor from recombinant Escherichia coli using thioredoxin as fusion partner
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Recombinant Expression of Mammalian Selenocysteine-Containing Thioredoxin Reductase and Other Selenoproteins in Escherichia coli
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High-level expression of soluble heterologous proteins in the cytoplasm of Escherichia coli by fusion to the bacteriophage Lambda head protein D
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