Fusions of elastin-like peptide (ELP) purification tags and self-cleaving inteins provide a powerful platform for purifying tagless recombinant proteins without the need for conventional packed-bed columns. A drawback to this method has been premature cleaving of the ELP tag during expression, before the purification procedure can take place. Here we demonstrate a split-intein method, where the self-cleaving intein is divided into two inactive segments during expression and purification. Spontaneous assembly of the purified intein segments then restores self-cleaving activity to deliver the tagless target protein.
CITATION STYLE
Shi, C., Han, T. C., & Wood, D. W. (2017). Purification of microbially expressed recombinant proteins via a dual ELP split intein system. In Methods in Molecular Biology (Vol. 1495). Humana Press Inc. https://doi.org/10.1007/978-1-4939-6451-2_2
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