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The germs Escherichia coli is still considered the first choice as a microbial cell factory for recombinant protein manufacturing, and affinity chromatography is by much the liked strategy for first filtration after protein expression and cell lysis. In this chapter, we define the approach to reveal and purify recombinant healthy proteins in E. coli identified with the first 2 metal-binding healthy proteins recommended as combination partners. Below we additionally explain the method for the production of proteins in the periplasm of E. coli marked with 2 SmbP variations that consist of the PelB or the TorA signal sequences for transportation via the Sec or the Tat path, respectively. Based on these techniques, we take into consideration CusF3H+ and SmbP exceptional alternatives as fusion proteins for the manufacturing of recombinant proteins in E. coli.
Source link: https://doi.org/10.1007/978-1-0716-0775-6_22
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