Fifteen related ligation-independent cloning vectors were constructed for high-throughput
cloning and purification of proteins. The vectors encode a TEV protease site for removal of …

The development of affinity-tag fusion technology in the mid-1980s provided a simple and
convenient method for the purification of arbitrary recombinant proteins through genetic …

Selective protein cleavage at methionine residues is a useful method for the production of
bacterially derived protein fragments containing an N-terminal cysteine residue required for …

Effective proteome-wide strategies that distinguish the N-termini of proteins from the N-
termini of their protease cleavage products would accelerate identification of the substrates …

We introduce a new method for the purification of recombinant proteins expressed in
Escherichia coli using self-cleaving elastin-like polypeptide (ELP) fusion tags without the …

When producing and purifying recombinant proteins it is of importance to minimize the
number of unit operations during the purification procedure. This is accomplished by …

Protein conjugates of high heterogeneity may contain species with significantly different
biological properties, and as a consequence, the focus on methods for production of …

Here, we present a cloning strategy for the production of recombinant proteins tagged with a
polyhistidine sequence that can be cleaved by the exopeptidase, DAPase. The method can …

Enzyme-catalyzed peptide ligation is a powerful tool for site-specific protein bioconjugation,
but stringent enzyme-substrate specificity limits its utility. We developed an approach for …

A modular series of versatile expression vectors is described for improved affinity purification
of recombinant fusion proteins. Special features of these vectors include (i) serial affinity tags …