UNIT 9.8 Immunoprecipitation

  1. Juan S. Bonifacino1,
  2. Esteban C. Dell'Angelica1,
  3. Timothy A. Springer2

Published Online: 1 MAY 2001

DOI: 10.1002/0471140864.ps0908s18

Current Protocols in Protein Science

Current Protocols in Protein Science

How to Cite

Bonifacino, J. S., Dell'Angelica, E. C. and Springer, T. A. 2001. Immunoprecipitation. Current Protocols in Protein Science. 18:9.8:9.8.1–9.8.28.

Author Information

  1. 1

    National Institute of Child Health and Human Development, Bethesda, Maryland

  2. 2

    Center for Blood Research, Harvard Medical School, Boston, Massachusetts

Publication History

  1. Published Online: 1 MAY 2001
  2. Published Print: DEC 1999


Immunoprecipitation is a technique in which an antigen is isolated by binding to a specific antibody attached to a sedimentable matrix. It is also used to analyze protein fractions separated by other biochemical techniques such as gel filtration or density gradient sedimentation. The source of antigen for immunoprecipitation can be unlabeled cells or tissues, metabolically or intrinsically labeled cells, or in-vitro-translated proteins. This unit describes a wide range of immunoprecipitation techniques, using either suspension or adherent cells lysed by various means (e.g., with and without detergent, using glass beads, etc.). Flow charts and figures give the user a clear-cut explanation of the options for employing the technology.