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Expression, Purification, and Antimicrobial Activity of S100A12
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Biochemistry
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JoVE Journal Biochemistry
Expression, Purification, and Antimicrobial Activity of S100A12

Expression, Purification, and Antimicrobial Activity of S100A12

DOI:
10.3791/55557-v

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11:10 min

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May 13, 2017

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, , , ,
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

Chapters

  • 00:05Title
  • 01:17Expression of S100A12
  • 03:20Purification of S100A12 Using Low Pressure Chromatography
  • 06:27Antimicrobial Activity Assays
  • 07:58Results: The Expression, Purification, and Antimicrobial Activity of S100A12
  • 09:42Conclusion

Summary

Automatic Translation

Automatic Translation

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.

Tags

S100A12Antimicrobial PeptideProtein ExpressionProtein PurificationAntimicrobial ActivityMetal SequestrationOligomerizationCalprotectinBL21 DE3 CellsAutoinduction MediaCentrifugationSonicationAffinity ChromatographySize Exclusion Chromatography

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