Soluble Expression of Recombinant Nerve Growth Factor in Cytoplasm of Escherichia coli

Soluble Expression of Recombinant Nerve Growth Factor in Cytoplasm of Escherichia coli.

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 β-NGF. In previous studies bacterial expression of hNGF demonstrated the feasibility of...

Co-expression of recombinant human nerve growth factor with trigger factor chaperone in E. coli

Nerve growth factor (NGF) is a neurotrophic factor that is functional in the survival, maintenance and differentiation of nervous system cells. This protein has three subunits, of which the beta subunit has the main activity. Its structure consists of a cysteine knot motif made up of beta strands linked by disulfide bonds. It can be used as a therapeutic agent in the treatment of many diseases....

Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli

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 hence recombinant technology is often the method of choice. Recombinant cell factories are constantly employed for the production of protein preparations bound for downstream purification and processing. Eschericia co...

Advances and challenges in recombinant protein expression in Escherichia coli

cloning and expression of human keratinocyte growth factor in escherichia coli for recombinant drug production

results cloning was confirmed by pcr and restriction digestion. rt-pcr and sds-page represented expression of kgf in e. coli. the optimized expression was achieved 16 hours after induction with 0.3 mm iptg at 37°c in luria broth (lb) containing kanamycin. the 18 kda protein was confirmed by western blotting, using anti-his antibodies. conclusions the result of the present study indicated that e...

CONSTRUCTION OF RECOMBINANT PLASMIDS FOR PERIPLASMIC EXPRESSION OF HUMAN GROWTH HORMONE IN ESCHERICHIA COLI UNDER T7 AND LAC PROMOTERS

In order to study the periplasmic expression of human growth hormone (hGH) in Escherichia coli, the related cDNA was inserted in two expression plasmids carrying pelB signal peptide, one with lac bacterial promoter and the other with a bacteriophage T7-based promoter. The recombinant plasmids were moved to TG1 and BL21 strains of E. coli, respectively. To induce the expression systems, IPTG and...