The development of self-cleaving fusion-tag technology has greatly simplified the purification of recombinant proteins at laboratory scale. The self-cleaving capability of these tags has recently been combined with additional purification tags to generate novel and convenient protein purification methods at a variety of scales. In this review, we describe some of these methods, and provide a rudimentary economic analysis of hypothetical large-scale applications. This work is expected to provide a rough outline for the evaluation of these methods for large-scale bioprocessing of a variety of products. © 2005 Banki and Wood, licensee BioMed Central Ltd.
CITATION STYLE
Banki, M. R., & Wood, D. W. (2005, November 11). Inteins and affinity resin substitutes for protein purification and scale up. Microbial Cell Factories. https://doi.org/10.1186/1475-2859-4-32
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