Proteins and peptides expressed in the prokaryotic system often form inclusion bodies.
Solubilization and refolding procedures can be used for their recovery, but this process …

Protein purification remains a central need for biotechnology. In recent years, a class of
aggregating tags has emerged, which offers a quick, cost‐effective and column‐free …

Protein fusion tags are indispensible tools used to improve recombinant protein expression
yields, enable protein purification, and accelerate the characterization of protein structure …

Eukaryotic proteins expressed in Escherichia coli often accumulate within the cell as
insoluble protein aggregates or inclusion bodies. The recovery of structure and activity from …

Many proteins that accumulate in the form of insoluble aggregates when they are
overproduced in Escherichia coli can be rendered soluble by fusing them to E. coli maltose …

Metal ions and complexes that hydrolyze peptides and proteins have become increasingly
important in recent years. These reagents have shown great promise for use in a variety of …

Advances in genetic engineering have made the production of biologically active
mammalian proteins from microbial cells a routine procedure. The main organisms for …

Expression as inclusion bodies in Escherichia coli is a widely used method for the large‐
scale production of therapeutic proteins that do not require post‐translational modifications …

PagP, a beta-barrel membrane protein found in Gram-negative bacteria, expresses robustly
in inclusion bodies when its signal sequence is removed. We have developed a new fusion …

The vast majority of protein purification is now done with cloned, recombinant proteins
expressed in a suitable host. The predominant host is Escherichia coli. Many, if not most …