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In this research, we present a recombinant strategy to make ACTH in Escherichia coli (E. coli). The SUMO-tagged fusion necessary protein had been cloned and expressed after induction with isopropyl-β-d-thiogalactopyranoside (IPTG) at 25 °C for 8 h. The fusion protein ended up being removed and purified by anion exchange chromatography, therefore the SUMO label ended up being afterwards eliminated by digestion with ubiquitin-like protease 1 (ULP1). Around 95.3 mg of recombinant ACTH with 94.2% purity