The massive waste of poly (ethylene terephthalate)(PET) that ends up in the landfills and
oceans and needs hundreds of years for degradation has attracted global concern. The poor …

Escherichia coli is one of the organisms of choice for the production of recombinant proteins.
Its use as a cell factory is well-established and it has become the most popular expression …

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 …

Pure, soluble and functional proteins are of high demand in modern biotechnology. Natural
protein sources rarely meet the requirements for quantity, ease of isolation or price and …

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

Background In the search for generic expression strategies for mammalian protein families
several bacterial expression vectors were examined for their ability to promote high yields of …

The fusion of a protein of interest to a large‐affinity tag, such as the maltose‐binding protein
(MBP), thioredoxin (TRX), or glutathione‐S‐transferase (GST), can be advantageous in …

Since the dawn of time, or at least the dawn of recombinant DNA technology (which for many
of today's scientists is the same thing), investigators have been cloning and expressing …

Strategies for growing protein crystals have for many years been essentially empirical, the
protein, once purified to a certain homogeneity, being mixed with a selection of …

Solubility of proteins on overexpression in Escherichia coli is a manifestation of the net effect
of several sequence‐dependent and sequence‐independent factors. This study aims to …