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Co-immunoprecipitation Analysis for the Detection of Protein–Protein Interactions in Yersinia pestis

  • Shiyang Cao
  • Zongmin Du
Protocol
Part of the Springer Protocols Handbooks book series (SPH)

Abstract

Co-immunoprecipitation is a classical method for the study of protein–protein and protein–DNA interactions, which is based on the specific recognition of antigens by antibodies (Sahr T, Buchrieser C: Methods Mol Biol 954:583–593, 2013). It is an effective method for determining the physiological interactions of two proteins under physiological conditions in intact cells. The protein–protein interactions identified by in vitro detection assays require further studies to confirm that they occur inside living cells. Fusing a small peptide tag, for instance, the FLAG-tag, to a protein of interest facilitates its co-immunoprecipitation using a commercially available anti-FLAG affinity gel. Compared with other methods for studying protein–protein interactions (such as pulldown assays and yeast two-hybrid screening), the protein–protein interactions identified by immunoprecipitation are generally an accurate reflection of the in vivo situation.

Key words

Interaction In vitro detection Protein Yersinia pestis 

References

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Copyright information

© Springer Nature Singapore Pte Ltd. 2018

Authors and Affiliations

  • Shiyang Cao
    • 1
  • Zongmin Du
    • 1
  1. 1.State Key Laboratory of Pathogen and BiosecurityBeijing Institute of Microbiology and EpidemiologyBeijingChina

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