نتایج جستجو برای: فاکتوررشداپیدرمیانسانی hegf
تعداد نتایج: 97 فیلتر نتایج به سال:
Human epidermal growth factor (hEGF) is a small, mitotic growth polypeptide that promotes the proliferation of various cells and is widely applied in clinical practices. However, high efficient expression of native hEGF in Escherichia coli has not been successful, since three disulfide bonds in monomer hEGF made it unable to fold into correct 3D structure using in vivo system. To tackle this pr...
Human Epidermal Growth Factor (hEGF) is a protein molecule with potent mitogenic activity, increasing the rate of wound and ulcer healing in different tissues of the human body. In recent years, the Center for Genetic Engineering and Biotechnology (CIGB) has carried out projects at the developmental stages for the application of hEGF in novel therapies. It is now necessary to increase productio...
Construction 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...
Paired human donor corneas (age, 73 +/- 12 yr), preserved in organ culture medium, were used to evaluate the effect of human epidermal growth factor (hEGF) on endothelial wound closure rate (WCR), on morphometric parameters (cell size, shape, and density), and on cell division in the wound area. The endothelium of the corneas was mechanically wounded (area, 4.9 +/- 0.9 mm2). For each pair, one ...
UNLABELLED The Auger electron-emitting radiopharmaceutical 111In-diethylenetriaminepentaacetic acid human epidermal growth factor (111In-DTPA-hEGF) binds the epidermal growth factor receptor (EGFR), is internalized, and translocates to the nucleus. The purpose of this study was to investigate the relationship between EGFR expression, DNA damage, and cytotoxicity in cells exposed to 111In-DTPA-h...
BACKGROUND We previously showed the usefulness of a fused protein of human pancreatic ribonuclease1 (hRNase1) with human epidermal growth factor (hEGF) for molecular targeting of EGF receptor (EGFR)-overexpressing cells. In this study, the mechanisms underlying the inhibition of cell growth by RNase-EGF fused proteins was confirmed. MATERIALS AND METHODS Des.1-7 hRNase1 was genetically fused ...
AIM To test the efficacy and safety of recombinant human epidermal growth factor (hEGF) on corneal re-epithelialisation following penetrating keratoplasty. METHODS A prospective, randomised, placebo controlled study was carried out in which patients were matched for diagnosis and received either hEGF ophthalmic solution (30 micrograms/ml or 100 micrograms/ml) or placebo in a double masked fas...
Purified human epidermal growth factor (hEGF) from urine promotes anchorage-independent cell growth in soft agar medium. This growth is enhanced by transforming growth factor-/} (TGF-/8), and is specifically inhibited by hEGF antiserum. Transforming growth factors of the a type (TGF-a), potentially present in normal human urine or urine from tumorbearing patients, also promote anchorage-indepen...
Human recombinant epidermal growth factor (hEGF) was evaluated in various corneal wound healing models in the rabbit. Human EGF accelerated epithelial wound healing in corneal reepithelialization, anterior-keratectomy, and alkali-burn models at concentrations of 10-500 micrograms/ml given four times daily (qid). In the corneal reepithelialization model, 100 micrograms/ml of hEGF qid produced a ...
125I-labeled human epidermal growth factor (hEGF) binds in a specific and saturable manner to human fibroblasts. At 37 degrees C, the cell-bound 125I-hEGF initially may be recovered in a native form by acid extraction; upon subsequent incubation, the cell-bound 125I-hEGF is degraded very rapidly, with the appearance in the medium of 125I-monoiodotyrosine. At 0 degrees C, cell-bound 125I-hEGF is...
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