Selected article for: "protein expression and recombinant protein expression"

Author: Oh, Seo-ho; Kim Cho, Young-Saeng; Lee, Ho-Bin; Lee, Sang-Mok; Kim, Whee-Soo; Hong, Liang; Cho, Chong-Su; Choi, Yun-Jaie; Kang, Sang-Kee
Title: Enhancement of antigen-specific humoral immune responses and protein solubility through conjugation of bacterial flagellin, Vibrio vulnificus FlaB, to the N-terminus of porcine epidemic diarrhea virus surface protein antigen S0
  • Document date: 2019_11_5
  • ID: q4p77ukw_25
    Snippet: We transformed each expression vector into E. coli BL21(DE3) and induced expression with IPTG. After cell disruption by sonication, soluble lysates were separated from insoluble lysates. Enhancing the solubility of each recombinant protein was deemed an important factor because we planned to utilize the soluble lysates for further experiments. To assess soluble expression, soluble and insoluble fractions of each recombinant protein were confirmed.....
    Document: We transformed each expression vector into E. coli BL21(DE3) and induced expression with IPTG. After cell disruption by sonication, soluble lysates were separated from insoluble lysates. Enhancing the solubility of each recombinant protein was deemed an important factor because we planned to utilize the soluble lysates for further experiments. To assess soluble expression, soluble and insoluble fractions of each recombinant protein were confirmed through SDS-PAGE followed by Coomassie Blue staining. S0 was expressed almost entirely as an insoluble protein, while 99% of flagellin was expressed as a soluble protein ( Fig. 1A and C) .

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