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Expression, Purification, and Antimicrobial Activity of S100A12
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Expression, Purification, and Antimicrobial Activity of S100A12

Article DOI: 10.3791/55557-v • 11:10 min • May 13th, 2017
May 13th, 2017 •
1, 1, 1, 2,3, 1,4
1Department of Life and Physical Sciences, Fisk University, 2Tennessee Valley Healthcare Systems, U. S. Dept. of Veterans Affairs, 3Department of Medicine - Division of Infectious Diseases, Vanderbilt University Medical School, 4Department of Biochemistry, Vanderbilt University

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Here, we present a method to express and purify S100A12 (calgranulin C). We describe a protocol to measure its antimicrobial activity against the human pathogen H. pylori.

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Expression Purification Antimicrobial Activity S100A12 Isolation Active Form Antimicrobial Assays Microbiology Field Role Of S100A12 Antimicrobial Peptide Pathogenic Bacteria Optimized Protocol High Yields Stable Pure S100A12 Dimer Bind And Sequester Nutrient Metals Oligomers Diminished Antimicrobial Activity In Vitro S100A Family Protein Calprotectin Size And Column Final Purification Steps Transform Competent BL21 DE3 Cells Plasmid Bacteria Micro Centrifuge Tube Heat-shock The Cells SOC M
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