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

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 …

Formation of inclusion bodies in bacterial hosts poses a major challenge for large scale
recovery of bioactive proteins. The process of obtaining bioactive protein from inclusion …

With the current biotherapeutic market dominated by antibody molecules, bispecific
antibodies represent a key component of the next-generation of antibody therapy. Bispecific …

Preparations enriched by a specific protein are rarely easily obtained from natural host cells.
Hence, recombinant protein production is frequently the sole applicable procedure. The …

Inclusion bodies produced in Escherichia coli are composed of densely packed denatured
protein molecules in the form of particles. Refolding of inclusion body proteins into bioactive …

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 …

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 …

A common limitation of recombinant protein production in bacteria is the formation of
insoluble protein aggregates known as inclusion bodies. The propensity of a given protein to …