期刊
CURRENT OPINION IN STRUCTURAL BIOLOGY
卷 26, 期 -, 页码 54-61出版社
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2014.04.006
关键词
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Engineered purification tags can facilitate very efficient purification of recombinant proteins, resulting in high yields and purities in a few standard steps. Over the years, many different purification tags have been developed, including short peptides, epitopes, folded protein domains, non-chromatographic tags and more recently, compound multifunctional tags with optimized capabilities. Although classic proteases are still primarily used to remove the tags from target proteins, new self-cleaving methods are gaining traction as a highly convenient alternative. In this review, we discuss some of these emerging trends, and examine their potential impacts and remaining challenges in recombinant protein research.
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