Proteins are now widely produced in diverse microbial cell factories. The Escherichia coli is
still the dominant host for recombinant protein production but, as a bacterial cell, it also has …

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 protein expression in Escherichia coli (E. coli) is simple, fast, inexpensive, and
robust, with the expressed protein comprising up to 50 percent of the total cellular protein …

Despite the availability of numerous gene fusion systems, recombinant protein expression in
Escherichia coli remains difficult. Establishing the best fusion partner for difficult‐to‐express …

Proteins do not naturally lend themselves to high-throughput analysis because of their
diverse physiochemical properties. Consequently, affinity tags have become indispensable …

Recombinant proteins are widely used today in many industries, including the
biopharmaceutical industry, and can be expressed in bacteria, yeasts, mammalian and …

Different species of microorganisms including yeasts, filamentous fungi and bacteria have
been used in the past 25 years for the controlled production of foreign proteins of scientific …

It has recently become clear that ribosomes are much more heterogeneous than previously
thought, with diversity arising from rRNA sequence and modifications, ribosomal protein …

Disulfide-rich peptides are the dominant component of most animal venoms. These peptides
have received much attention as leads for the development of novel therapeutic agents and …

Tags are frequently used in the expression of recombinant proteins to improve solubility and
for affinity purification. A large number of tags have been developed for protein production …