Selection of a system for successful recombinant protein production is important. The aim of this study wasto produce high levels of human interleukin-2 (hIL-2) in soluble form. To this end, the pET32a vector inEscherichia coli BL21 (DE3) was used as an expression system, since it was previously used for the productionof mouse IL-2 in soluble form. The results indicated that c...

Escherichia coli is one of the most widely used hosts for the production of recombinant proteins but insoluble expression of heterologous proteins is a major bottleneck in production of recombinant proteins in E. coli. In vitro refolding of inclusion body into proteins with native conformations is a solution for this problem but there is a need for optimization of condition for each protein spe...

Microbial host systems remain the most efficient and cost-effective chassis for biotherapeutics production. Escherichia coli is often preferred due to ease of cloning, scale-up, high product yields, importantly, cultivation. E. experience difficulties in producing biologically active therapeutics such as Fab fragments, which require protein folding subsequent three-dimensional structure develop...

Fibroblast growth factor 15 (Fgf15) is the mouse orthologue of human FGF19. Fgf15 is highly expressed in the ileum and functions as an endocrine signal to regulate liver function, including bile acid synthesis, hepatocyte proliferation and insulin sensitivity. In order to fully understand the function of Fgf15, methods are needed to produce pure Fgf15 protein in the prokaryotic system. However,...

BACKGROUND Escherichia coli has been most widely used for the production of valuable recombinant proteins. However, over-production of heterologous proteins in E. coli frequently leads to their misfolding and aggregation yielding inclusion bodies. Previous attempts to refold the inclusion bodies into bioactive forms usually result in poor recovery and account for the major cost in industrial pr...

The properties of molecular chaperones in protein-assisted refolding were examined in vitro using recom-binant human cytosolic chaperones hsp9O, hsc7O, hsp7O and hdj-1, and unfolded 3-galactosidase as the sub-strate. In the presence of hsp7O (hsc7O), hdj-1 and either ATP or ADP, denatured 3-galactosidase refolds and forms enzymatically active tetramers. Interactions between hsp9O and non-native...

A number of aspects of the refolding of denatured rabbit muscle creatine kinase have been studied. Addition of substrates has no effect on the rate or extent of regain of activity. The changes in protein fluorescence during refolding broadly parallel the regain of activity. A study of the susceptibility of the enzyme to proteolysis during refolding indicates that there is no significant accumul...

The book Heat Shock Proteins (HSP) in Cellular Communication and Signaling Volume 26 provides the most comprehensive highlight insight of expression, function therapeutic activity HSP signaling pathways. Using an integrative approach to understanding various HSP-mediated pathways response a variety stressors including hyperthermia, or metabolic changes produced by physical exercise psychologica...