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A Short Polypeptide Marker Sequence Useful for Recombinant Protein Identification and Purification

Bio/Technology volume 6, pages 1204–1210 (1988)Cite this article

Abstract

A small hydrophilic peptide of eight amino acids (AspTyrLysAspAspAspAspLys) was engineered onto the N-terminus of a variety of recombinant lymphokines for the purpose of aiding in their detection and purification from yeast supernatants or E. coli extracts. An antibody specific for the first four amino acids of this sequence was used as a detection reagent and for immunoaffinity purification of products under mild conditions. Because of the small size of the peptide moiety and its hydrophilic nature, the proteins were unaffected by its presence and retained a high level of biological activity. In addition, it was possible to remove the peptide via an enzymatic cleavage procedure using enterokinase.

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Author notes

  1. Randell T. Libby

    Present address: Departments of Genetics, SK-50, and Pathology, SM-30, University of Washington, Seattle, WA, 98195

Authors and Affiliations

  1. Immunex Corporation, 51 University Street, Seattle, Washington, 98101

    Thomas P. Hopp, Kathryn S. Prickett, Virginia L. Price, Carl J. March, Douglas Pat Cerretti, David L. Urdal & Paul J. Conlon

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  1. Thomas P. Hopp
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Hopp, T., Prickett, K., Price, V. et al. A Short Polypeptide Marker Sequence Useful for Recombinant Protein Identification and Purification. Nat Biotechnol 6, 1204–1210 (1988). https://doi.org/10.1038/nbt1088-1204

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  • DOI: https://doi.org/10.1038/nbt1088-1204

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