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10.1016/j.pep.2014.08.010

http://scihub22266oqcxt.onion/10.1016/j.pep.2014.08.010
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C4466898!4466898!25149396
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suck abstract from ncbi


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pmid25149396      Protein+Expr+Purif 2014 ; 103 (ä): 75-83
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  • Production and characterization of thirteen human Type-I interferon-? subtypes #MMPMID25149396
  • Kuruganti S; Accavitti-Loper MA; Walter MR
  • Protein Expr Purif 2014[Nov]; 103 (ä): 75-83 PMID25149396show ga
  • Thirteen human interferon-? (IFN?) subtypes were expressed in E. coli and purified using an N-terminal affinity tag from the prodomain of subtilisn. IFN? subtypes were expressed in soluble form and purified from cell lysates or refolded and purified from inclusion bodies. Proteins produced by either protocol exhibited biological activities equal to or greater than commercially prepared IFN? preparations. The IFN?s were used to produce an anti-IFN?16 antibody (MAb-1B12) that specifically neutralized the biological activity of IFN?16, but not the 12 other IFN?s. Using MAb-1B12, and a previously generated IFNAR1/IFNAR2-FChk heterodimer, an assay was developed to determine total type I IFN biological activity and IFN?16-derived biological activity in an unknown sample.
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