Cloning and Expression of Recombinant Human Endostatin in Periplasm of Escherichia coli Expression System
Cloning and Expression of Recombinant Human Endostatin in Periplasm of Escherichia coli Expression System
نویسندگان: نصرت اله ضرغامی , محمد پورحسن مقدم , جلال عبدالعلیزاده , پوران کریمی
کلمات کلیدی: Angiogenesis
Endostatin
Signal peptide
E. coli
Gene expression
Periplasm
نشریه: 951 , 2 , 6 , 2016
| نویسنده ثبت کننده مقاله |
نصرت اله ضرغامی |
| مرحله جاری مقاله |
تایید نهایی |
| دانشکده/مرکز مربوطه |
مرکز تحقیقات سل و بیماری های ریوی |
| کد مقاله |
59142 |
| عنوان فارسی مقاله |
Cloning and Expression of Recombinant Human Endostatin in Periplasm of Escherichia coli Expression System |
| عنوان لاتین مقاله |
Cloning and Expression of Recombinant Human Endostatin in Periplasm of Escherichia coli Expression System |
| ناشر |
6 |
| آیا مقاله از طرح تحقیقاتی و یا منتورشیپ استخراج شده است؟ |
بلی |
| عنوان نشریه (خارج از لیست فوق) |
|
| نوع مقاله |
Original Article |
| نحوه ایندکس شدن مقاله |
ایندکس شده سطح سه – Scopus |
| آدرس لینک مقاله/ همایش در شبکه اینترنت |
http://apps.webofknowledge.com/full_record.do?product=WOS&search_mode=GeneralSearch&qid=6&SID=U2fv2uWYMPhuMT5JSne&page=1&doc=1 |
| Purpose: Recombinant human endostatin (rhEs) is an angiogenesis inhibitor which is used
as a specific drug in the treatment of non-small-cell lung cancer. In the current research, we
developed an efficient method for expressing soluble form of the rhEs protein in the
periplasmic space of Escherichia coli via fusing with pelB signal peptide.
Methods: The human endostatin (hEs) gene was amplified using synthetic (hEs) gene as a
template; then, cloned and expressed under T7 lac promoter. IPTG was used as an inducer
for rhEs expression. Next, the osmotic shock was used to extraction of protein from the
periplasmic space. The presence of rhEs in the periplasmic space was approved by SDSPAGE
and Western blotting.
Results: The results show the applicability of pelB fusion protein system usage for secreting
rhEs in the periplasm of E. coli in the laboratory scale. The rhEs represents approximately
35 % (0.83mg/l) of the total cell protein.
Conclusion: The present study apparently is the first report of codon-optimized rhEs
expression as a fusion with pelB signal peptide. The results presented the successful
secretion of soluble rhEs to the periplasmic space. |
| نام فایل |
تاریخ درج فایل |
اندازه فایل |
دانلود |
| Cloning and expression of recombinant human endostatin in periplasm of Escherichia coli expression system.pdf | 1395/08/06 | 832525 | دانلود |
| Cloning and expression of recombinant human endostatin in periplasm of Escherichia coli expression system.pdf | 1395/08/06 | 832525 | دانلود |