Expression and purification of human epidermal growth factor (hEGF) fused with GB1
نویسندگان
چکیده
منابع مشابه
cloning, expression, and cost effective purification of authentic human epidermal growth factor with high activity
background epidermal growth factor (egf) plays a fundamental role in the healing of wounds relating to skin damage, the cornea, and the gastrointestinal tract. objectives the aim of this study is the cloning, expression, and purification of recombinant human egf (rhegf), and an assessment of its activity. materials and methods in the present experimental study, a synthetic pet28a (+) -hegf cons...
متن کاملThe Periplasmic Expression of Recombinant Human Epidermal Growth Factor (hEGF) in Escherichia coli
Expression of recombinant eukaryotic proteins in Escherichia coli often results in the formation of inclusion bodies. In the case of disulfide-bonded proteins such as hEGF, inclusion body formation can be anticipated if the protein is produced in the bacterial cytosol. The consequence is improper folding which results in aggregation. Proper folding and solubility of such protein are pre-requisi...
متن کاملConstruction of Yeast Recombinant Expression Vector Containing Human Epidermal Growth Factor (hEGF).
PURPOSE The objective of this study was construction of recombinant hEGF-pPIC9 which may be used for expression of recombinant hEGF in following studies. METHODS EGF cDNA was purchased from Genecopoeia Company and used for PCR amplification. Prior to ligation, the PCR product and pPIC9 vector was digested with EcoRI and XhoI and ligated in pPIC9 vector and subjected to colony PCR screening an...
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EGFR is a key molecule in cancer cells. EGFR signaling was shown to promote tumor cell proliferation and survival, invasion and angiogenesis and mediate resistance to treatment, including ionizing radiation in preclinical models. We extracted proteins from astrocytoma (III and IV) oligodendroglioma(IV) tumors and normal brain tissues and then evaluated the protein purity by Bradford test ...
متن کاملHigh-level expression and purification of human epidermal growth factor with SUMO fusion in Escherichia coli.
Human epidermal growth factor (hEGF) can stimulate the division of various cell types and has potential clinical applications. However, the high expression of active hEGF in Escherichia coli has not been successful, as the protein contains three intra-molecular disulfide bonds that are difficult to form correctly in the bacterial intracellular environment. To solve this problem, we fused the hE...
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ژورنال
عنوان ژورنال: Biotechnology & Biotechnological Equipment
سال: 2016
ISSN: 1310-2818,1314-3530
DOI: 10.1080/13102818.2016.1166984