Today, proteins are typically overexpressed using solubility-enhancing fusion tags that allow
for affinity chromatographic purification and subsequent removal by site-specific protease …

Biologically active proteins are useful for studying the biological functions of genes and for
the development of therapeutic drugs and biomaterials in a biotechnology industry …

Recent advances in generating active proteins through refolding of bacterial inclusion body
proteins are summarized in conjunction with a short overview on inclusion body isolation …

Expression of heterologous proteins in E. coli often leads to the formation of protein
aggregates known as inclusion bodies (IBs). Inclusion body aggregates pose a major hurdle …

Many recombinant eukaryotic proteins tend to form insoluble aggregates called inclusion
bodies, especially when expressed in Escherichia coli. We report the first application of the …

Research and industrial demands for recombinant proteins continue to increase over time
for their broad applications in structural and functional studies and as therapeutic agents …

Site-specific protein cleavage is essential for many protein-production protocols and
typically requires proteases. We report the development of a chemical protein-cleavage …

One major bottleneck in protein production in Escherichia coli for structural genomics
projects is the formation of insoluble protein aggregates (inclusion bodies). The efficient …

Advancements in peptide fusion technologies to maximize the protein production has taken
a big leap to fulfill the demands of post-genomics era targeting elucidation of …

The production of recombinant proteins in a large scale is important for protein functional
and structural studies, particularly by using Escherichia coli over-expression systems; …