Attachment of oligo‐histidine tag (His‐tag) to the protein N‐or C‐terminus is a good example
of early and successful protein engineering to design a unique and generalized purification …

The science, art, and practice of protein purification have been with us for more than a
century, yet, in many respects, the field is only now evolving past its adolescent roots. New …

Mass spectrometry and peptide-centric approaches are powerful techniques for the
identification of differentially expressed proteins. Despite enormous improvements in MS …

His-tagging is the most widespread and versatile strategy used to purify recombinant
proteins for biochemical and structural studies. Recombinant DNA methods are first used to …

Over-expression and purification of soluble and functional proteins remain critical
challenges for many aspects of biomolecular research. To address this, we have developed …

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 …

Covering both new and traditional topics in the purification and analysis of recombinant
proteins, this volume demonstrates how to overcome problems in protein research and …

A positively charged protein domain, Zbasic, can be used as a general purification tag to
achieve efficient recovery of recombinantly produced target proteins using cation-exchange …

The present review deals with the use of combinatorial ligand libraries, composed by
hexapeptides, in the capture and concentration of the low‐abundance proteome. This …

Recombinant proteins typically include one or more affinity tags to facilitate purification
and/or detection. Expression constructs with affinity tags often include an engineered …