Progress in our understanding of several biological processes promises to broaden the
usefulness of Escherichia coli as a tool for gene expression. There is an expanding choice …

Aggregation results in the formation of inclusion bodies, amyloid fibrils and folding
aggregates. Substantial data support the hypothesis that partially folded intermediates are …

E. coli is most preferred system used for the production of recombinant proteins in bacteria
and the availability of improved genetic tools/methods are making it more valuable than …

The many advantages of Escherichia coli have ensured that it remains a valuable host for
the efficient, cost-effective and high-level production of heterologous proteins. Here, we …

The demands of structural and functional genomics for large quantities of soluble, properly
folded proteins in heterologous hosts have been aided by advancements in the field of …

Recombinant proteins are often expressed in the form of insoluble inclusion bodies in
bacteria. To facilitate refolding of recombinant proteins obtained from inclusion bodies, 0.1 to …

Since immobilized metal ion affinity chromatography (IMAC) was first introduced, several
variants of this method and many other metal affinity-based techniques have been devised …

Protein aggregation is an ordinary consequence of thermal stress. In recombinant bacteria,
the over-expression of plasmid-encoded genes triggers transcription of heat-shock genes …

Many fields of science and industry depend on efficient production of active protein using
heterologous expression in Escherichia coli. The solubility of proteins upon expression is …

Tobacco etch virus NIa proteinase (TEV protease) is an important tool for the removal of
fusion tags from recombinant proteins. Production of TEV protease in Escherichia coli has …