UNIT 10.11A Immunoaffinity Chromatography

  1. Timothy A. Springer

Published Online: 1 MAY 2001

DOI: 10.1002/0471142727.mb1011as36

Current Protocols in Molecular Biology

Current Protocols in Molecular Biology

How to Cite

Springer, T. A. 2001. Immunoaffinity Chromatography. Current Protocols in Molecular Biology. 36:IV:10.11A:10.11.1–10.11.9.

Author Information

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

Publication History

  1. Published Online: 1 MAY 2001
  2. Published Print: OCT 1996


Immunoaffinity purification is a powerful technique for isolating proteins. Purifications of 10,000-fold or more can often be achieved in one step. This unit describes the isolation of soluble or membrane-bound protein antigens from cells or homogenized tissue by immunoaffinity chromatography. The technique involves the elution of a single protein from an immunoaffinity column after prior elution of nonspecifically adsorbed proteins. An alternate protocol describes the use of batch purification of antigens which can shorten the column loading time.