Enhanced Expression of Recombinant Activin A in Escherichia coli by Optimization of Induction Parameters
نویسندگان
چکیده مقاله:
Activin A is a member of the transforming growth factor β super family. Because of its extensive clinical usages, its recombinant production is beneficial. In this study, activin A was expressed in E. coli using the pET 21a expression vector. The optimization of the activin A production in E. coli was done by using the response surface methodology (RSM). At this stage, the effect of IPTG and lactose concentration as inducers on protein production was investigated. The effect of different post-induction time and temperature on protein production was then studied in two strains of E. coli (BL21(DE3) and BL21(DE3) plysS). For enhanced expression, the optimum IPTG and lactose concentrations were 1.5 mM and 0% W/V respectively. In the DE3 strain, the optimum post-induction time and temperature were 10 hours and 30°C respectively while in DE3 (plysS) these were 4 hours and 35°C respectively
منابع مشابه
The Expression of Human Granulocyte Macrophage Colony Stimulating Factor by Heat-Induction in Escherichia coli
A self-regulated high-copy number plasmid containing chloramphenicol resistant gene, for the production of recombinant proteins under the regulation of bacteriophage ?pL promoter, was constructed. The designed 5024 base pair expression plasmid contained a heat sensitive repressor cI857 coding gene to regulate the function of ?pL promoter under heat shock induction. Using the constructed vector,...
متن کاملoptimization of auto-induction conditions for the heterologous expression of a maltogenic amylase in escherichia coli
background and objectives: auto-induction is usually employed to achieve high cell density and overproduction of proteins with a simple and low-cost operation. the efficiency of heterologous protein expression in escherichia coli is determined by different parameters. interactions between these parameters usually complicate the identification of those that contribute more to the improvement of ...
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 کاملOptimization of Cloning Conditions for high-level Production of Recombinant Mouse Interleukin-2 in Escherichia coli
Backgrounds and objectives: Interleukin 2 (IL-2) secreted by activated CD4+ T cells has been known as a major mediator in both adaptive and native immune system due to a board range of effects on different cells in the immunity system (1-6). Methods: cDNA synthesis was performed using gene- specific primers designed by Gene Runner software after RNA extraction of mouse splenocytes. PCR pro...
متن کاملEnhanced Production of Insulin-Like Growth Factor I Protein in Escherichia coli by optimization of five key factors
Abstract Human insulin-like growth factor I (hIGF-I) is a kind of growth factor with clinical significance in medicine. The major objective of this study is over- production of recombinant human insulin-like growth factor I( rhIGF-I) through a developed process by recruiting effective factors in order to achieve the most recombinant protein. Up to now E. coli expression system has been widely us...
متن کاملمنابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ذخیره در منابع من قبلا به منابع من ذحیره شده{@ msg_add @}
عنوان ژورنال
دوره 29 شماره 2
صفحات 105- 111
تاریخ انتشار 2018-04-01
با دنبال کردن یک ژورنال هنگامی که شماره جدید این ژورنال منتشر می شود به شما از طریق ایمیل اطلاع داده می شود.
میزبانی شده توسط پلتفرم ابری doprax.com
copyright © 2015-2023