Fusion expression is a common practice for recombinant protein production. Some fusion
tags confer solubility on the target protein whereas others provide affinity handles that …

Fusion constructs are used to improve the properties of or impart novel functionality to
proteins for biotechnological applications. The biochemical characteristics of enzymes or …

Protein fusion technology has enormously facilitated the efficient production and purification
of individual recombinant proteins. The use of genetically engineered affinity and solubility …

Here we report the use of a self-assembling protein cage to sequester and solubilize
recombinant proteins which are usually trafficked to insoluble inclusion bodies. Our results …

The rapid provision of purified native protein underpins both structural biology and the
development of new biopharmaceuticals. The dominance of Escherichia coli as a cellular …

Background Formation of inclusion bodies poses a major hurdle in recovery of bioactive
recombinant protein from Escherichia coli. Urea and guanidine hydrochloride have routinely …

Selective cleavage of peptides and proteins is an important procedure in biochemistry and
molecular biology. The half-life for the uncatalyzed hydrolysis of amide bonds is 350-500 …

Overexpression of recombinant proteins in bacteria frequently produces inactive, insoluble
inclusion bodies instead of active, soluble proteins. It is not entirely clear why high …

Protein purification typically involves expressing a recombinant gene comprising a target
protein fused to a suitable affinity tag. After purification, it is often desirable to remove the …

Several fusion tail systems have been developed to promote efficient recovery and
purification of recombinant proteins from crude cell extracts or culture media. In these …