Efficient Expression of Bioactive Human Leptin in Escherichia coli in Soluble Fusion Form
نویسندگان
چکیده
منابع مشابه
Expression and Purification of Soluble form of Human Parathyroid Hormone (rhPTH1-34) by Trx Tag in E. coli
Background: Parathyroid Hormone (PTH) is secreted by parathyroid glands and controls the level of calcium in bones and kidney. PTH is a small polypeptide with 84 amino acids, but the first 34 amino acids of which are enough for hormone biological activity and can be used in the treatment of Osteoporosis. The expression efficiency of recombinant human parathyroid hormone rhPTH (1-34) or Teripara...
متن کاملSoluble 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 b-NGF. In previous studies bacterial expression of hNGF demonstrated the feasibility o...
متن کاملhigh-level soluble expression and one-step purification of htlv-i p19 protein in escherichia coli by fusion expression
expression of htlv-i p19 protein in an escherichia coli expression system always leads to the formation of inclusion body. solubilisation and refolding of the inclusion bodies is complex, time consuming and difficult during large-scale preparation. this study aimed to express and purify a soluble form of recombinant htlv-i p19 protein in an e. coli expression system. the synthetic dna encoding ...
متن کاملMycobacterium tuberculosis HspX/EsxS Fusion Protein: Gene Cloning, Protein Expression, and Purification in Escherichia coli
Background: The purpose of this study was to clone, express, and purify a novel multidomain fusion protein of Micobacterium tuberculosis (Mtb) in a prokaryotic system. Methods: An hspX/esxS gene construct was synthesized and ligated into a pGH plasmid, E. coli TOP10 cells were transformed, and the vector was purified. The vector containing the construct and pET-21b (+) plasmid were digested ...
متن کاملEfficient Process Development of Recombinant Human Granulocyte Colony-Stimulating Factor (rh-GCSF) Production in Escherichia coli
Background: The protein hormone granulocyte colony-stimulating factor (GCSF) stimulates the production of white blood cells and plays an important role in medical treatment of cancer patients. Methods: An efficient process was developed for heterologous expression of human GCSF in E. coli BL21 (DE3). The feeding rate was adjusted to achieve the maximum attainable specific growth rate under crit...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Indian Journal of Clinical Biochemistry
سال: 2010
ISSN: 0970-1915,0974-0422
DOI: 10.1007/s12291-010-0066-2