Selected article for: "affinity column and recombinant protein"
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_13
    Snippet: The soluble fractions of S0-F and F-S0, which were expressed in the presence of tig, were purified using affinity chromatography on a Ni 2+ -NTA column. Purified samples were dialyzed against phosphate buffered saline (PBS) at 4°C three times and subsequently concentrated using Amicon ultra-15 centrifugal filters (Merck, Germany). Contaminating lipopolysaccharide (LPS) was further removed by using an endotoxin removal spin column (Thermo Scienti.....
    Document: The soluble fractions of S0-F and F-S0, which were expressed in the presence of tig, were purified using affinity chromatography on a Ni 2+ -NTA column. Purified samples were dialyzed against phosphate buffered saline (PBS) at 4°C three times and subsequently concentrated using Amicon ultra-15 centrifugal filters (Merck, Germany). Contaminating lipopolysaccharide (LPS) was further removed by using an endotoxin removal spin column (Thermo Scientific, USA), and the residual LPS content of each recombinant protein was determined using the ToxinSensor Chromogenic LAL Endotoxin Assay Kit (Genescript, USA). The LPS levels of each recombinant protein were below 0.03 EU/mL and 0.0075 EU per dose.

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