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. 1994 Apr;16(4):730-5.

Immunoaffinity purification of FLAG epitope-tagged bacterial alkaline phosphatase using a novel monoclonal antibody and peptide elution

B L Brizzard  1 , R G Chubet, D L Vizard
Affiliations
  • PMID: 8024796

Immunoaffinity purification of FLAG epitope-tagged bacterial alkaline phosphatase using a novel monoclonal antibody and peptide elution

B L Brizzard et al. Biotechniques. 1994 Apr.

Abstract

The FLAG epitope is an eight amino acid peptide (AspTyrLysAspAspAspAspLys) that is useful for immunoaffinity purification of fusion proteins. A monoclonal antibody (anti-FLAG M1) that binds the FLAG epitope in a calcium-dependent manner and requires an N-terminal FLAG sequence has been described previously. We describe the use of a second anti-FLAG monoclonal antibody (anti-FLAG M2) in immunoaffinity purification of N-terminal Met-FLAG and C-terminal FLAG fusion to bacterial alkaline phosphatase. Although binding of an anti-FLAG M2 monoclonal antibody to the FLAG epitope is not calcium-dependent, bound fusion proteins can be eluted by competition with FLAG peptide.

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