Soluble expression of recombinant nerve growth factor in cytoplasm of escherichia coli

ABSTRACT

Background: Pivotal roles of Nerve growth factor [NGF] in the development and survival of both neuronal and non-neuronal cells indicate its potential for the treatment of neurodegenerative diseases. However, investigation of NGF deficits in different diseases requires the availability of properly folded human beta-NGF. In previous studies bacterial expression of hNGF demonstrated the feasibility of its overproduction. However, known limitations in the use of E. coli as an expression host for a protein with three intra-chain disulfide bonds were evident