Aptamer-Based Precipitation as an Alternative to the Conventional Immunoprecipitation for Purification of Target Proteins 


Vol. 35,  No. 9, pp. 2665-2668, Sep.  2014
10.5012/bkcs.2014.35.9.2665


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  Abstract

Aptamers are oligonucleotides or peptide molecules that are able to bind to their specific target molecules with high affinity via molecular recognition. In this study, we present development of aptamer-based precipitation assays (or simply aptamoprecipitation) for His-tagged proteins and thrombin to compare their purification efficiency with other conventional affinity precipitation methods. A crosslinking method was employed to immobilize thiol-functionalized aptamers onto the surface of polystyrene resins, enabling them to specifically bind to His-tag and to thrombin, respectively. The resulting aptamer-functionalized resins were successfully applied via a one-step experiment to purification of His-tagged proteins from complex E. coli and to thrombin extraction, exhibiting superior or at least comparable purification results to the conventional immobilized metal affinity precipitation or immunoprecipitation.

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  Cite this article

[IEEE Style]

S. Song, Y. S. Cho, S. Lee, S. S. Hah, "Aptamer-Based Precipitation as an Alternative to the Conventional Immunoprecipitation for Purification of Target Proteins," Bulletin of the Korean Chemical Society, vol. 35, no. 9, pp. 2665-2668, 2014. DOI: 10.5012/bkcs.2014.35.9.2665.

[ACM Style]

Seongeun Song, Yea Seul Cho, Sung-Jae Lee, and Sang Soo Hah. 2014. Aptamer-Based Precipitation as an Alternative to the Conventional Immunoprecipitation for Purification of Target Proteins. Bulletin of the Korean Chemical Society, 35, 9, (2014), 2665-2668. DOI: 10.5012/bkcs.2014.35.9.2665.

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ISSN(Print) 0253-2964
ISSN(Online) 1229-5949