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 …

Highly purified recombinant proteins in large quantities are valuable material for
biochemical and structural studies. To achieve this goal, versatile tools were developed to …

Protein fusion tags are indispensible tools used to improve recombinant protein expression
yields, enable protein purification, and accelerate the characterization of protein structure …

Escherichia coli is the most widely used heterologous protein expression system. However,
this system remains a challenge due to the low solubility of proteins, insufficient yield, 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 …

Addition of an affinity tag is a useful method for differentiating recombinant proteins
expressed in bacterial and eukaryotic expression systems from the background of total …

The soluble expression of heterologous proteins in Escherichia coli remains a serious
bottleneck in protein production. Although alteration of expression conditions can sometimes …

Addition of an affinity tag is a useful method for differentiating recombinant proteins
expressed in bacterial and eukaryotic expression systems from the background of total …

Protein fusion technology has had a major impact on the efficient production and purification
of individual recombinant proteins. The use of genetically engineered affinity and solubility …

Recombinant proteins are generally fused with solubility enhancer tags to improve the
folding and solubility of the target protein of interest. However, the fusion protein strategy …