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The novel Fh8 and H fusion partners for soluble protein expression in Escherich...

The Escherichia coli host system is an advantageous choice for simple and inexpensive recombinant protein production but it still presents bottlenecks at expressing soluble proteins from other organisms. Several efforts have been taken to overcome E. coli limitations, including the use of fusion partners that improve protein expression and solubility. New fusion technologies are emerging to complement the tradi...

The Fh8 tag : a fusion partner for simple and cost-effective protein purificati...

Downstream processing is still a major bottleneck in recombinant protein production representing most of its costs. Hence, there is a continuing demand of novel and cost-effective purification processes aiming at the recovery of pure and active target protein. In this work, a novel purification methodology is presented, using the Fh8 solubility enhancer tag as fusion handle. The binding properties of Fh8 tag to...

A novel adjuvant-free H fusion system for the production of recombinant immunog...

The production of recombinant antigens in Escherichia coli and specific polyclonal antibodies for diagnosis and therapy is still a challenge for world-wide researchers. Several different strategies have been explored to improve both antigen and antibody production, all of them depending on a successful expression and immunogenicity of the antigen. Gene fusion technology attempted to address these challenges: fu...

Cloning and expression of Clostridium thermocellum CBM3 in Pichia pastoris

Development of a novel fusion system for antibiotic-free Escherichia coli recom...