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Challenges and opportunities in the purification of recombinant tagged proteins

机译：纯化重组标签蛋白的挑战和机遇

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摘要

The purification of recombinant proteins by affinity chromatography is one of the most efficient strategies due to the high recovery yields and purity achieved. However, this is dependent on the availability of specific affinity adsorbents for each particular target protein. The diversity of proteins to be purified augments the complexity and number of specific affinity adsorbents needed, and therefore generic platforms for the purification of recombinant proteins are appealing strategies. This justifies why genetically encoded affinity tags became so popular for recombinant protein purification, as these systems only require specific ligands for the capture of the fusion protein through a pre-defined affinity tag tail. There is a wide range of available affinity pairs "tag-ligand" combining biological or structural affinity ligands with the respective binding tags. This review gives a general overview of the well-established "tag-ligand" systems available for fusion protein purification and also explores current unconventional strategies under development.
机译：通过亲和层析纯化重组蛋白是最有效的策略之一，因为它具有很高的回收率和纯度。但是，这取决于每种特定靶蛋白的特异性亲和吸附剂的可用性。待纯化蛋白质的多样性增加了所需的特异性亲和吸附剂的复杂性和数量，因此用于纯化重组蛋白质的通用平台是有吸引力的策略。这证明了为什么遗传编码的亲和标签在重组蛋白纯化中变得如此流行，因为这些系统仅需要特定的配体即可通过预定的亲和标签尾部捕获融合蛋白。有大量可用的亲和对“标签-配体”，其将生物学或结构亲和配体与各自的结合标签结合在一起。这篇综述给出了可用于融合蛋白纯化的公认的“标签-配体”系统的一般概述，并探讨了当前正在开发的非常规策略。

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