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JOURNAL ARTICLE
RESEARCH SUPPORT, NON-U.S. GOV'T
Split intein facilitated tag affinity purification for recombinant proteins with controllable tag removal by inducible auto-cleavage.
Journal of Chromatography. A 2011 May 7
Purification tags are robust tools that can be used to purify a variety of target proteins. However, tag removal remains an expensive and significant issue that must be resolved. Based on the affinity and the trans-splicing activity between the two domains of Ssp DnaB split-intein, a novel approach for tag affinity purification of recombinant proteins with controllable tag removal by inducible auto-cleavage has been developed. This system provides a new affinity method and avoids premature splicing of the intein fused proteins expressed in host cells. The affinity matrix can be reused. In addition, this method is compatible with his-tag affinity purification technique. Our methods provide the insights for establishing a novel recombinant protein preparation system.
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