Escherichia coli is the most widely used heterologous protein expression system. However,
this system remains a challenge due to the low solubility of proteins, insufficient yield, and …

The ability to assemble a target protein from a series of peptide fragments, either synthetic or
biosynthetic in origin, enables the covalent structure of a protein to be modified in an …

Since the dawn of time, or at least the dawn of recombinant DNA technology (which for many
of today's scientists is the same thing), investigators have been cloning and expressing …

We introduce a new method for purifying recombinant proteins expressed in bacteria using a
highly specific, inducible, self-cleaving protease tag. This tag is comprised of the Vibrio …

Recombinant proteins are becoming increasingly important for industrial applications, where
Escherichia coli is the most widely used bacterial host for their production. However, the …

Protein refolding is still a bottleneck for large-scale production of valuable proteins
expressed as inclusion bodies in Escherichia coli. Usually biologically active proteins …

The expression and harvesting of proteins from insoluble inclusion bodies by solubilization
and refolding is a technique commonly used in the production of recombinant proteins. To …

During expression of many recombinant proteins, off-pathway association of partially folded
intermediates into inclusion bodies competes with productive folding. A common assumption …

The aims of high‐throughput (HTP) protein production systems are to obtain well‐expressed
and highly soluble proteins, which are preferred candidates for use in structure–function …

Background The engineering of fusion proteins has become increasingly important and
most recently has formed the basis of many biosensors, protein purification systems, and …